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Conserved domains on  [gi|446585239|ref|WP_000662585|]
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MULTISPECIES: patatin-like phospholipase family protein [Bacillus]

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

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List of domain hits

 Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-246 6.00e-90

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


:

Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 266.77  E-value: 6.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   1 MKEPKIGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLA-----------TVFKRK 69
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWrsldrrdlfdlSLPRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  70 YYLDFTVPKMGFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGR 149
Cdd:COG1752   82 LRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239 150 LLVDGGVIDRIPVSVVKELGADIVIAVDVSPIKvnGEVTSIYDVIMQSIEIMQHELvMNRQIA---SDLMMRPAVEQFSS 226
Cdd:COG1752  162 LYVDGGVVNNLPVDPARALGADRVIAVDLNPPL--RKLPSLLDILGRALEIMFNSI-LRRELAlepADILIEPDLSGISL 238

                        250       260
                 ....*....|....*....|
gi 446585239 227 RAFTNIEDIIRVGEVEAEKH 246
Cdd:COG1752  239 LDFSRAEELIEAGYEAARRA 258
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-246 6.00e-90

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 266.77  E-value: 6.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   1 MKEPKIGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLA-----------TVFKRK 69
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWrsldrrdlfdlSLPRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  70 YYLDFTVPKMGFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGR 149
Cdd:COG1752   82 LRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239 150 LLVDGGVIDRIPVSVVKELGADIVIAVDVSPIKvnGEVTSIYDVIMQSIEIMQHELvMNRQIA---SDLMMRPAVEQFSS 226
Cdd:COG1752  162 LYVDGGVVNNLPVDPARALGADRVIAVDLNPPL--RKLPSLLDILGRALEIMFNSI-LRRELAlepADILIEPDLSGISL 238

                        250       260
                 ....*....|....*....|
gi 446585239 227 RAFTNIEDIIRVGEVEAEKH 246
Cdd:COG1752  239 LDFSRAEELIEAGYEAARRA 258
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 6-178 5.71e-76

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: 228.31  E-value: 5.71e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   6 IGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKRKY--YLDFTVPKMGFIA 83
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVlrLLDLSASRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  84 GKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGRLLVDGGVIDRIPVS 163
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 446585239 164 VVKELGADIVIAVDV 178
Cdd:cd07228  161 VARALGADIVIAVDL 175
PRK10279 PRK10279
patatin-like phospholipase RssA;
1-245 6.95e-49

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 163.34  E-value: 6.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   1 MKEPKIGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAagCNveRLYKLAT-VFKRKYY-----LDF 74
Cdd:PRK10279   1 MRKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYA--CD--RLSALEDwVTSFSYWdvlrlMDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  75 TVPKMGFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGRLLVDG 154
Cdd:PRK10279  77 SWQRGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239 155 GVIDRIPVSVVKELGADIVIAVDVS-----------PIKVN---------------------------GEVTSIYDVIMQ 196
Cdd:PRK10279 157 AVVNPVPVSLTRALGADIVIAVDLQhdahlmqqdllSFNVSeensengdslpwharlkerlgsittrrAVTAPTAMEIMT 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446585239 197 -SIEIMQHELVMNRQIAS--DLMMRPAVEQFSSRAFTNIEDIIRVGEVEAEK 245
Cdd:PRK10279 237 tSIQVLENRLKRNRMAGDppDILIQPVCPQISTLDFHRAHAAIAAGQLAVEK 288
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 8-165 7.42e-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: 103.07  E-value: 7.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239    8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKRKYYLDFTVPKM-------- 79
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRAlsllallr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   80 ------GFIAGKRVKDMIKMFTYNKNLEEL-----------------DIPTAVVATDILKGEKVVFTSGPVADAVRASIS 136
Cdd:pfam01734  81 gligegGLFDGDALRELLRKLLGDLTLEELaarlslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*....
gi 446585239  137 VPGVFVPEKVNGRLLVDGGVIDRIPVSVV 165
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
 
Name Accession Description Interval E-value
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-246 6.00e-90

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 266.77  E-value: 6.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   1 MKEPKIGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLA-----------TVFKRK 69
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGYSADELEELWrsldrrdlfdlSLPRRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  70 YYLDFTVPKMGFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGR 149
Cdd:COG1752   82 LRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239 150 LLVDGGVIDRIPVSVVKELGADIVIAVDVSPIKvnGEVTSIYDVIMQSIEIMQHELvMNRQIA---SDLMMRPAVEQFSS 226
Cdd:COG1752  162 LYVDGGVVNNLPVDPARALGADRVIAVDLNPPL--RKLPSLLDILGRALEIMFNSI-LRRELAlepADILIEPDLSGISL 238

                        250       260
                 ....*....|....*....|
gi 446585239 227 RAFTNIEDIIRVGEVEAEKH 246
Cdd:COG1752  239 LDFSRAEELIEAGYEAARRA 258
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 6-178 5.71e-76

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: 228.31  E-value: 5.71e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   6 IGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKRKY--YLDFTVPKMGFIA 83
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVlrLLDLSASRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  84 GKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGRLLVDGGVIDRIPVS 163
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 446585239 164 VVKELGADIVIAVDV 178
Cdd:cd07228  161 VARALGADIVIAVDL 175
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 6-178 1.41e-70

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: 214.72  E-value: 1.41e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   6 IGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFK--RKYYLDFTVPKMGFIA 83
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRStdLKALSDLTIPTAGLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  84 GKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGRLLVDGGVIDRIPVS 163
Cdd:cd07205   81 GDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVD 160

                        170
                 ....*....|....*
gi 446585239 164 VVKELGADIVIAVDV 178
Cdd:cd07205  161 VLRELGADIIIAVDL 175
PRK10279 PRK10279
patatin-like phospholipase RssA;
1-245 6.95e-49

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 163.34  E-value: 6.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   1 MKEPKIGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAagCNveRLYKLAT-VFKRKYY-----LDF 74
Cdd:PRK10279   1 MRKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYA--CD--RLSALEDwVTSFSYWdvlrlMDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  75 TVPKMGFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGRLLVDG 154
Cdd:PRK10279  77 SWQRGGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239 155 GVIDRIPVSVVKELGADIVIAVDVS-----------PIKVN---------------------------GEVTSIYDVIMQ 196
Cdd:PRK10279 157 AVVNPVPVSLTRALGADIVIAVDLQhdahlmqqdllSFNVSeensengdslpwharlkerlgsittrrAVTAPTAMEIMT 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446585239 197 -SIEIMQHELVMNRQIAS--DLMMRPAVEQFSSRAFTNIEDIIRVGEVEAEK 245
Cdd:PRK10279 237 tSIQVLENRLKRNRMAGDppDILIQPVCPQISTLDFHRAHAAIAAGQLAVEK 288
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 6-176 6.03e-42

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: 142.87  E-value: 6.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   6 IGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYK--LATVFKRKYYLDFTVPKMGFIA 83
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPDEMAEllLSLERKDFWMFWDPPLRGGLLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  84 GKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGRLLVDGGVIDRIPVS 163
Cdd:cd07210   81 GDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPFD 160

                        170
                 ....*....|....
gi 446585239 164 -VVKELGADIVIAV 176
Cdd:cd07210  161 aLRPEIERILYHHV 174
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 6-178 1.68e-40

Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are 60% identical to each other. 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 homologous 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 PNPLA6 and PNPLA7 from Homo sapiens, YMF9 from Yeast, and Swiss Cheese protein (sws) from Drosophila melanogaster.


Pssm-ID: 132864 [Multi-domain]  Cd Length: 306  Bit Score: 141.77  E-value: 1.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   6 IGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKRKY------YLDFTVPKM 79
Cdd:cd07225   16 IALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERNISRMKQRAREWAKDMtsiwkkLLDLTYPIT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  80 GFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVP--EKVNGRLLVDGGVI 157
Cdd:cd07225   96 SMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPlcDPKDGHLLMDGGYI 175

                        170       180
                 ....*....|....*....|.
gi 446585239 158 DRIPVSVVKELGADIVIAVDV 178
Cdd:cd07225  176 NNLPADVARSMGAKTVIAIDV 196
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 8-201 7.56e-36

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: 127.02  E-value: 7.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCN--VERLYKL------ATVFKRK---YYLDFtv 76
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPeaVERLEKLwrelsrEDVFLRGlldRALDF-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  77 pkmgfiagkrvkdmikmftynKNLEELDIPTA---VVATDILKGEKVVFTSGPVA---DAVRASISVPGVFVPEKVNGRL 150
Cdd:cd07209   79 ---------------------DTLRLLAILFAglvIVAVNVLTGEPVYFDDIPDGilpEHLLASAALPPFFPPVEIDGRY 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446585239 151 LVDGGVIDRIPVSVVKELGADIVIAVDVSPIKVNGEVTSIYDVImqsIEIM 201
Cdd:cd07209  138 YWDGGVVDNTPLSPAIDLGADEIIVVSLSDKGRDDRKGTPPTTL---IEIL 185
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 6-178 2.33e-35

Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. 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 family includes NTE1 from fungi.


Pssm-ID: 132865 [Multi-domain]  Cd Length: 269  Bit Score: 127.22  E-value: 2.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   6 IGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKR------KYYLDFTVPKM 79
Cdd:cd07227   11 IGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAREADLVPIFGRAKKFAGrmasmwRFLSDVTYPFA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  80 GFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEKVVFTSGPVADAVRASISVPGVFVPEKVNGRLLVDGGVIDR 159
Cdd:cd07227   91 SYTTGHEFNRGIWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSDNGSMLLDGGYMDN 170

                        170
                 ....*....|....*....
gi 446585239 160 IPVSVVKELGADIVIAVDV 178
Cdd:cd07227  171 LPVSPMRSLGIRDIFAVDV 189
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 8-164 1.50e-31

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: 115.07  E-value: 1.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKRKYYLDFTVPKMGFIAG--- 84
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGYSAADIKDILKETDFAKLLDSPVGLLFLLPSlfk 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  85 -----------KRVKDMIKMFTYNKNL--------EELDIPTAVVATDILKGEKVVFtSG------PVADAVRASISVPG 139
Cdd:cd07207   82 egglykgdaleEWLRELLKEKTGNSFAtsllrdldDDLGKDLKVVATDLTTGALVVF-SAettpdmPVAKAVRASMSIPF 160

                        170       180
                 ....*....|....*....|....*.
gi 446585239 140 VFVP-EKVNGRLLVDGGVIDRIPVSV 164
Cdd:cd07207  161 VFKPvRLAKGDVYVDGGVLDNYPVWL 186
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 8-176 6.35e-31

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: 112.82  E-value: 6.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKR--KYYLDFTVPKMGFIAGK 85
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSRevRLRFDGAFPPTGRLLGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  86 RVKDMIKmFTYNKNLEELDIPTAVVATDILKGEKVV---FTSGPVADAVRASISVPGVF--VPEKVNGRLLVDGGVIDRI 160
Cdd:cd07198   81 LRQPLLS-ALPDDAHEDASGKLFISLTRLTDGENVLvsdTSKGELWSAVRASSSIPGYFgpVPLSFRGRRYGDGGLSNNL 159

                        170
                 ....*....|....*.
gi 446585239 161 PvsvVKELGADIVIAV 176
Cdd:cd07198  160 P---VAELGNTINVSP 172
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 8-165 7.42e-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: 103.07  E-value: 7.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239    8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGCNVERLYKLATVFKRKYYLDFTVPKM-------- 79
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRAlsllallr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   80 ------GFIAGKRVKDMIKMFTYNKNLEEL-----------------DIPTAVVATDILKGEKVVFTSGPVADAVRASIS 136
Cdd:pfam01734  81 gligegGLFDGDALRELLRKLLGDLTLEELaarlslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*....
gi 446585239  137 VPGVFVPEKVNGRLLVDGGVIDRIPVSVV 165
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 8-174 1.00e-19

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju 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: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 85.74  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGI-PIHMIAGSSMGALIGTFYAAG------------CNVERLYKLATVFKRKYYLDf 74
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIrPFDLVIGVSAGALNAASYLSGqrgralrintkyATDPRYLGLRSLLRTGNLFD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  75 tvpkMGFIAGkRVKDMIKMFTYNKnLEELDIPTAVVATDILKGEKVVFTSGPVAD----AVRASISVPGVFVPEKVNGRL 150
Cdd:cd07208   80 ----LDFLYD-ELPDGLDPFDFEA-FAASPARFYVVATDADTGEAVYFDKPDILDdlldALRASSALPGLFPPVRIDGEP 153

                        170       180
                 ....*....|....*....|....*.
gi 446585239 151 LVDGGVIDRIPVSVVKELGAD--IVI 174
Cdd:cd07208  154 YVDGGLSDSIPVDKAIEDGADkiVVI 179
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
1-176 1.31e-19

Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 85.60  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   1 MKEPKIGLALGSGGAKG-FAHiGVIKVLREAGIPIHMIAGSSMGALIGTFYAAGcNVERLYKLATVF-KRKYYLDFtvpk 78
Cdd:COG4667    1 SNMMKTALVLEGGGMRGiFTA-GVLDALLEEGIPFDLVIGVSAGALNGASYLSR-QPGRARRVITDYaTDPRFFSL---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  79 MGFIAGKRVKDMIKMF-TYNKNLEELDIPTA--------VVATDILKGEKVVFTSGPVA----DAVRASISVPGVFVPEK 145
Cdd:COG4667   75 RNFLRGGNLFDLDFLYdEIPNELLPFDFETFkasprefyVVATNADTGEAEYFSKKDDDydllDALRASSALPLLYPPVE 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446585239 146 VNGRLLVDGGVIDRIPVSVVKELGADIVIAV 176
Cdd:COG4667  155 IDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 8-175 8.92e-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: 53.19  E-value: 8.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGI--PIHMIAGSSMGALIGTFyaagcnverlykLATVFkrkyyldftvpkmgfiagk 85
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAAT------------LYPPS------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  86 rVKDMIKMFtyNKNLEELDIPTAVVATDILKGEKVV---FTS-GPVADAVRASISVPGVF--------VPEKVN----GR 149
Cdd:cd01819   50 -SSLDNKPR--QSLEEALSGKLWVSFTPVTAGENVLvsrFVSkEELIRALFASGSWPSYFglippaelYTSKSNlkekGV 126

                        170       180
                 ....*....|....*....|....*...
gi 446585239 150 LLVDGGVIDRIPVSVVK--ELGADIVIA 175
Cdd:cd01819  127 RLVDGGVSNNLPAPVLLrpGRGVTLTIS 154
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 8-157 5.41e-06

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: 46.56  E-value: 5.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVL-REAG--IPIH----MIAGSSMGALIgtfyAAGcnverlyklatVFKRKYyldftvpkmg 80
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELeKRLGkpSRIAdlfdLIAGTSTGGII----ALG-----------LALGRY---------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  81 fiagkRVKDMIKMFTynKNLEELDIPTAVVATDILKGEKVVFTSG-----------PVADAVRASISVPGVFVPEKV--- 146
Cdd:cd07199   57 -----SAEELVELYE--ELGRKIFPRVLVTAYDLSTGKPVVFSNYdaeepdddddfKLWDVARATSAAPTYFPPAVIesg 129

                        170
                 ....*....|..
gi 446585239 147 -NGRLLVDGGVI 157
Cdd:cd07199  130 gDEGAFVDGGVA 141
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 5-51 3.16e-05

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: 44.56  E-value: 3.16e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446585239   5 KIGLALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYA 51
Cdd:cd07232   67 RTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAALLC 113
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 8-168 4.87e-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: 43.74  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGtfyaagcnverlyklatvfkrkyyldftvpkmGFIAGKRV 87
Cdd:cd07206   72 LMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVA--------------------------------ALLGTHTD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  88 KDMIKMFT----YNKNLEELDIptAVVATDILKGEKVV--FTSgP---VADAVRASISVPGVFVP----------EKVN- 147
Cdd:cd07206  120 EELIGDLTfqeaYERTGRIINI--TVAPAEPHQNSRLLnaLTS-PnvlIWSAVLASCAVPGVFPPvmlmaknrdgEIVPy 196

                        170       180
                 ....*....|....*....|...
gi 446585239 148 --GRLLVDGGVIDRIPVSVVKEL 168
Cdd:cd07206  197 lpGRKWVDGSVSDDLPAKRLARL 219
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 8-198 7.54e-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 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: 43.05  E-value: 7.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGiP-----IHMIAGSSMGALIGTFYAAGCN---VERLYKLAT--VFKRKyYLDFTVP 77
Cdd:cd07213    5 LSLDGGGVKGIVQLVLLKRLAEEF-PsfldqIDLFAGTSAGSLIALGLALGYSprqVLKLYEEVGlkVFSKS-SAGGGAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585239  78 KMGFIAGKRVKDMIKMFTYNKNLEELDIPTAVVATDILKGEK--------VVFTSGP--------VADAVRASISVPGVF 141
Cdd:cd07213   83 NNQYFAAGFLKAFAEVFFGDLTLGDLKRKVLVPSFQLDSGKDdpnrrwkpKLFHNFPgepdldelLVDVCLRSSAAPTYF 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446585239 142 VPekVNGrlLVDGGVIDRIPVSVVKELgadiVIAVDVSPIKVNgevtsiyDVIMQSI 198
Cdd:cd07213  163 PS--YQG--YVDGGVFANNPSLCAIAQ----AIGEEGLNIDLK-------DIVVLSL 204
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 8-51 1.97e-03

Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana.


Pssm-ID: 132869  Cd Length: 323  Bit Score: 38.97  E-value: 1.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTFYA 51
Cdd:cd07231   71 LLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIA 114
Pat_TGL3_like cd07229
Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG ...
 8-49 2.86e-03

Triacylglycerol lipase 3; Triacylglycerol lipase 3 (TGL3) are responsible for all the TAG lipase activity of the lipid particle. Triacylglycerol (TAG) lipases are also necessary for the mobilization of TAG stored in lipid particles. TGL3 contains the consensus sequence motif GXSXG, which is found in lipolytic enzymes. This family includes Tgl3p from Saccharomyces cerevisiae.


Pssm-ID: 132867  Cd Length: 391  Bit Score: 38.44  E-value: 2.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALIGTF 49
Cdd:cd07229   86 LVLQGGSIFGLCHLGVVKALWLRGLLPRIITGTATGALIAAL 127
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 8-46 2.88e-03

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: 38.74  E-value: 2.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446585239   8 LALGSGGAKGFAHIGVIKVLREAGIPIHMIAGSSMGALI 46
Cdd:cd07230   76 LLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIV 114
 
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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