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Conserved domains on  [gi|658549260|ref|WP_029741684|]
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MULTISPECIES: patatin-like phospholipase RssA [Enterobacter]

Protein Classification

patatin family protein( domain architecture ID 10013475)

uncharacterized patatin family protein similar to neuropathy target esterase (NTE)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10279 PRK10279
patatin-like phospholipase RssA;
1-299 0e+00

patatin-like phospholipase RssA;


:

Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 624.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   1 MRKVKIGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVRSFSYWDVLRLMDLSWQR 80
Cdd:PRK10279   1 MRKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  81 GGLLRGERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVDGGVVN 160
Cdd:PRK10279  81 GGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 161 PVPISLTRAMGADIVIAVDLQHDAHLMQQDLMPVNLQS-EDAEGEKLAWHERLRGRIGRMAARRSVAAPTAIEIMTTSIQ 239
Cdd:PRK10279 161 PVPVSLTRALGADIVIAVDLQHDAHLMQQDLLSFNVSEeNSENGDSLPWHARLKERLGSITTRRAVTAPTAMEIMTTSIQ 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 240 VLENRLKRNRMAGDPPDILIQPYCPQISTLDFHRAEAAIAAGSLAVEKKMDELLPFVQTA 299
Cdd:PRK10279 241 VLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQLAVEKKMDELLPLVRTN 300
 
Name Accession Description Interval E-value
PRK10279 PRK10279
patatin-like phospholipase RssA;
1-299 0e+00

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 624.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   1 MRKVKIGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVRSFSYWDVLRLMDLSWQR 80
Cdd:PRK10279   1 MRKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  81 GGLLRGERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVDGGVVN 160
Cdd:PRK10279  81 GGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 161 PVPISLTRAMGADIVIAVDLQHDAHLMQQDLMPVNLQS-EDAEGEKLAWHERLRGRIGRMAARRSVAAPTAIEIMTTSIQ 239
Cdd:PRK10279 161 PVPVSLTRALGADIVIAVDLQHDAHLMQQDLLSFNVSEeNSENGDSLPWHARLKERLGSITTRRAVTAPTAMEIMTTSIQ 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 240 VLENRLKRNRMAGDPPDILIQPYCPQISTLDFHRAEAAIAAGSLAVEKKMDELLPFVQTA 299
Cdd:PRK10279 241 VLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQLAVEKKMDELLPLVRTN 300
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 6-180 7.25e-95

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: 277.62  E-value: 7.25e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   6 IGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVRSFSYWDVLRLMDLSWQRGGLLR 85
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVLRLLDLSASRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  86 GERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVDGGVVNPVPIS 165
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 658549260 166 LTRAMGADIVIAVDL 180
Cdd:cd07228  161 VARALGADIVIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-291 4.93e-86

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 258.29  E-value: 4.93e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   1 MRKVKIGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACG-KLPELETWVRSFSYWDVLRL------ 73
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGySADELEELWRSLDRRDLFDLslprrl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  74 --MDLSWQRGGLLRGERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGY 151
Cdd:COG1752   82 lrLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 152 WLVDGGVVNPVPISLTRAMGADIVIAVDLQHDAHlmqqdlmpvnlqsedaegeklawherlrgrigrmaarrsvAAPTAI 231
Cdd:COG1752  162 LYVDGGVVNNLPVDPARALGADRVIAVDLNPPLR----------------------------------------KLPSLL 201

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 232 EIMTTSIQVLENRLKRNRMAGDPPDILIQPYCPQISTLDFHRAEAAIAAGSLAVEKKMDE 291
Cdd:COG1752  202 DILGRALEIMFNSILRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 8-164 3.67e-30

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: 112.70  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260    8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPE------LETWVRSFSYWDVLRLMDLSWQRG 81
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEeiedllLELDLNLFLSLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   82 GLLRGERVFNQ------FRQVMPLEDFTDC-----------------QMPFGAVATNLSTGRELWLTEGDIHLAVRASCS 138
Cdd:pfam01734  81 GLIGEGGLFDGdalrelLRKLLGDLTLEELaarlslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*.
gi 658549260  139 MPGLMAPVPHNGYWLVDGGVVNPVPI 164
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPV 186
 
Name Accession Description Interval E-value
PRK10279 PRK10279
patatin-like phospholipase RssA;
1-299 0e+00

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 624.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   1 MRKVKIGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVRSFSYWDVLRLMDLSWQR 80
Cdd:PRK10279   1 MRKIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  81 GGLLRGERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVDGGVVN 160
Cdd:PRK10279  81 GGLLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 161 PVPISLTRAMGADIVIAVDLQHDAHLMQQDLMPVNLQS-EDAEGEKLAWHERLRGRIGRMAARRSVAAPTAIEIMTTSIQ 239
Cdd:PRK10279 161 PVPVSLTRALGADIVIAVDLQHDAHLMQQDLLSFNVSEeNSENGDSLPWHARLKERLGSITTRRAVTAPTAMEIMTTSIQ 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 240 VLENRLKRNRMAGDPPDILIQPYCPQISTLDFHRAEAAIAAGSLAVEKKMDELLPFVQTA 299
Cdd:PRK10279 241 VLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQLAVEKKMDELLPLVRTN 300
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 6-180 7.25e-95

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: 277.62  E-value: 7.25e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   6 IGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVRSFSYWDVLRLMDLSWQRGGLLR 85
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVLRLLDLSASRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  86 GERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVDGGVVNPVPIS 165
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 658549260 166 LTRAMGADIVIAVDL 180
Cdd:cd07228  161 VARALGADIVIAVDL 175
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-291 4.93e-86

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 258.29  E-value: 4.93e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   1 MRKVKIGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACG-KLPELETWVRSFSYWDVLRL------ 73
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGySADELEELWRSLDRRDLFDLslprrl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  74 --MDLSWQRGGLLRGERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGY 151
Cdd:COG1752   82 lrLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 152 WLVDGGVVNPVPISLTRAMGADIVIAVDLQHDAHlmqqdlmpvnlqsedaegeklawherlrgrigrmaarrsvAAPTAI 231
Cdd:COG1752  162 LYVDGGVVNNLPVDPARALGADRVIAVDLNPPLR----------------------------------------KLPSLL 201

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 232 EIMTTSIQVLENRLKRNRMAGDPPDILIQPYCPQISTLDFHRAEAAIAAGSLAVEKKMDE 291
Cdd:COG1752  202 DILGRALEIMFNSILRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 6-180 7.37e-60

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: 188.52  E-value: 7.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   6 IGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPE--LETWVRSFSYWDVLRlmDLSWQRGGL 83
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEeiEERAKLRSTDLKALS--DLTIPTAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  84 LRGERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVDGGVVNPVP 163
Cdd:cd07205   79 LRGDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLP 158

                        170
                 ....*....|....*..
gi 658549260 164 ISLTRAMGADIVIAVDL 180
Cdd:cd07205  159 VDVLRELGADIIIAVDL 175
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 6-176 6.57e-39

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: 136.32  E-value: 6.57e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   6 IGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLP-ELETWVRSFSYWDVLRLMDLSWqRGGLL 84
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGISPdEMAELLLSLERKDFWMFWDPPL-RGGLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  85 RGERVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVDGGVVNPVPI 164
Cdd:cd07210   80 SGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPF 159

                        170
                 ....*....|..
gi 658549260 165 SLTRAMGADIVI 176
Cdd:cd07210  160 DALRPEIERILY 171
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 6-179 1.08e-30

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: 117.12  E-value: 1.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   6 IGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGK-----LPELETWVRSFSYWdVLRLMDLSWQR 80
Cdd:cd07225   16 IALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEERnisrmKQRAREWAKDMTSI-WKKLLDLTYPI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  81 GGLLRGeRVFNQ-FRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPV--PHNGYWLVDGG 157
Cdd:cd07225   95 TSMFSG-AAFNRsIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPLcdPKDGHLLMDGG 173

                        170       180
                 ....*....|....*....|..
gi 658549260 158 VVNPVPISLTRAMGADIVIAVD 179
Cdd:cd07225  174 YINNLPADVARSMGAKTVIAID 195
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 8-164 3.67e-30

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: 112.70  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260    8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPE------LETWVRSFSYWDVLRLMDLSWQRG 81
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEeiedllLELDLNLFLSLIRKRALSLLALLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   82 GLLRGERVFNQ------FRQVMPLEDFTDC-----------------QMPFGAVATNLSTGRELWLTEGDIHLAVRASCS 138
Cdd:pfam01734  81 GLIGEGGLFDGdalrelLRKLLGDLTLEELaarlslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*.
gi 658549260  139 MPGLMAPVPHNGYWLVDGGVVNPVPI 164
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPV 186
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 8-178 7.85e-30

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: 110.89  E-value: 7.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVRSFSYWDVLRLMDLSWQRGGLLRGe 87
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGRLLG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  88 RVFNQFRQVMPLEDFTDCQMPFGAVATNLSTGREL---WLTEGDIHLAVRASCSMPGLMAPVP--HNGYWLVDGGVVNPV 162
Cdd:cd07198   80 ILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVlvsDTSKGELWSAVRASSSIPGYFGPVPlsFRGRRYGDGGLSNNL 159

                        170
                 ....*....|....*.
gi 658549260 163 PISltrAMGADIVIAV 178
Cdd:cd07198  160 PVA---ELGNTINVSP 172
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 6-180 3.05e-29

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: 112.20  E-value: 3.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   6 IGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYAC-GKLPELETWVRSF-----SYWDVlrLMDLSWQ 79
Cdd:cd07227   11 IGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAReADLVPIFGRAKKFagrmaSMWRF--LSDVTYP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  80 RGGLLRGER----VFNQFRQVMpLEDFtdcQMPFGAVATNLSTGRELWLTEGDIHLAVRASCSMPGLMAPVPHNGYWLVD 155
Cdd:cd07227   89 FASYTTGHEfnrgIWKTFGNTH-IEDF---WIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSDNGSMLLD 164

                        170       180
                 ....*....|....*....|....*
gi 658549260 156 GGVVNPVPISLTRAMGADIVIAVDL 180
Cdd:cd07227  165 GGYMDNLPVSPMRSLGIRDIFAVDV 189
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 8-196 3.35e-27

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: 105.45  E-value: 3.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLP---ELETWVRSFSYWDVLRLmdlswqrgGLL 84
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPEaveRLEKLWRELSREDVFLR--------GLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  85 RGERVFNQfrqvmpLEDFTDCQMPFGAVATNLSTGRELWLTEGDIHL---AVRASCSMPGLMAPVPHNGYWLVDGGVVNP 161
Cdd:cd07209   73 DRALDFDT------LRLLAILFAGLVIVAVNVLTGEPVYFDDIPDGIlpeHLLASAALPPFFPPVEIDGRYYWDGGVVDN 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 658549260 162 VPISLTRAMGADIVIAVDLQHDAHLMQQDLMPVNL 196
Cdd:cd07209  147 TPLSPAIDLGADEIIVVSLSDKGRDDRKGTPPTTL 181
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
5-178 4.92e-27

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 106.40  E-value: 4.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   5 KIGLALGSGAARGwshI---GVINALNKMGIDVDIVAGCSIGSLVGSAYACGKlPEletwvRSF-SYWDVL---RLMdlS 77
Cdd:COG4667    5 KTALVLEGGGMRG---IftaGVLDALLEEGIPFDLVIGVSAGALNGASYLSRQ-PG-----RARrVITDYAtdpRFF--S 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  78 WQRggLLRGERVFNQ-------FRQVMPL--EDFTDCQMPFGAVATNLSTGRELWLT----EGDIHLAVRASCSMPGLMA 144
Cdd:COG4667   74 LRN--FLRGGNLFDLdflydeiPNELLPFdfETFKASPREFYVVATNADTGEAEYFSkkddDYDLLDALRASSALPLLYP 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 658549260 145 PVPHNGYWLVDGGVVNPVPISLTRAMGADIVIAV 178
Cdd:COG4667  152 PVEIDGKRYLDGGVADSIPVREAIRDGADKIVVI 185
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 8-176 4.18e-20

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: 87.66  E-value: 4.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGIDV-DIVAGCSIGSLVGSAYACGKLPeletwvRSFSYWDVL----RLMDL-SWQRG 81
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPfDLVIGVSAGALNAASYLSGQRG------RALRINTKYatdpRYLGLrSLLRT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  82 GLLRG-ERVFNQ---FRQVMPLEDFTDCQMPFGAVATNLSTGRELWLTEGDIH----LAVRASCSMPGLMAPVPHNGYWL 153
Cdd:cd07208   75 GNLFDlDFLYDElpdGLDPFDFEAFAASPARFYVVATDADTGEAVYFDKPDILddllDALRASSALPGLFPPVRIDGEPY 154

                        170       180
                 ....*....|....*....|....*
gi 658549260 154 VDGGVVNPVPISLTRAMGAD--IVI 176
Cdd:cd07208  155 VDGGLSDSIPVDKAIEDGADkiVVI 179
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 8-166 6.43e-15

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: 71.54  E-value: 6.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACG-KLPEL-----ETWVRSF--SYWDVLRLMDLSWQ 79
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALLALGySAADIkdilkETDFAKLldSPVGLLFLLPSLFK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  80 RGGLLRGERVFNQFRQVM----------PLEDFTDCQ--MPFGAVATNLSTGRELWLTEGD-----IHLAVRASCSMPGL 142
Cdd:cd07207   82 EGGLYKGDALEEWLRELLkektgnsfatSLLRDLDDDlgKDLKVVATDLTTGALVVFSAETtpdmpVAKAVRASMSIPFV 161

                        170       180
                 ....*....|....*....|....*
gi 658549260 143 MAPVP-HNGYWLVDGGVVNPVPISL 166
Cdd:cd07207  162 FKPVRlAKGDVYVDGGVLDNYPVWL 186
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 5-147 5.71e-07

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: 50.34  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   5 KIGLALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGsAYACGKLPE------LETWVRSF-SYWDVLRLMDLS 77
Cdd:cd07232   67 RTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVA-ALLCTRTDEelkqllVPELARKItACEPPWLVWIPR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  78 WQRGGLLRGERVFNqfRQVMpleDFTDCQMPFgAVATNLsTGREL-----------------WLTEGD--IHLAVRASCS 138
Cdd:cd07232  146 WLKTGARFDSVEWA--RTCC---WFTRGSMTF-EEAYER-TGRILnisvvpadphsptillnYLTSPNctIWSAVLASAA 218


                 ....*....
gi 658549260 139 MPGLMAPVP 147
Cdd:cd07232  219 VPGILNPVV 227
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 8-177 9.06e-07

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: 47.80  E-value: 9.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGI--DVDIVAGCSIGSLVGSAYAcgklpeletwVRSFSywdVLRLMDLSWQRggLLR 85
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLldCVTYLAGTSGGAWVAATLY----------PPSSS---LDNKPRQSLEE--ALS 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  86 GERVFnqfrqvmpleDFTDCQMPFGAVATNLSTGRELWltegdihLAVRASCSMPGLMAPVP------------HNGYWL 153
Cdd:cd01819   66 GKLWV----------SFTPVTAGENVLVSRFVSKEELI-------RALFASGSWPSYFGLIPpaelytsksnlkEKGVRL 128

                        170       180
                 ....*....|....*....|....*.
gi 658549260 154 VDGGVVNPVPISLTRA--MGADIVIA 177
Cdd:cd01819  129 VDGGVSNNLPAPVLLRpgRGVTLTIS 154
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 8-218 1.67e-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: 45.67  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELetwvrsfsywdvlrLMDLSWQrggllrge 87
Cdd:cd07206   72 LMLSGGASLGLFHLGVVKALWEQDLLPRVISGSSAGAIVAALLGTHTDEEL--------------IGDLTFQ-------- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260  88 rvfnqfrqvmplEDFTDcqmpfgavatnlsTGREL-----------------WLTEGD--IHLAVRASCSMPG------L 142
Cdd:cd07206  130 ------------EAYER-------------TGRIInitvapaephqnsrllnALTSPNvlIWSAVLASCAVPGvfppvmL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549260 143 MA------PVPH--NGYWlVDGGVVNPVPIS-LTRAMG---------------------ADIVIAVDLQ-HDAHLMQQDL 191
Cdd:cd07206  185 MAknrdgeIVPYlpGRKW-VDGSVSDDLPAKrLARLYNvnhfivsqtnphvvpflqeysGDITIIPPFSfSNPLKLLSNP 263

                        250       260       270
                 ....*....|....*....|....*....|.
gi 658549260 192 MPVNLQSEDAEGEKLAW----HERLRGRIGR 218
Cdd:cd07206  264 SEDELQRLILEGERATWpkieMIRTQTRISR 294
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 8-69 1.12e-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: 40.28  E-value: 1.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVRSFSYWD 69
Cdd:cd07230   76 LLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGD 137
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 8-63 1.69e-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: 39.36  E-value: 1.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 658549260   8 LALGSGAARGWSHIGVINALNKMGIDVDIVAGCSIGSLVGSAYACGKLPELETWVR 63
Cdd:cd07231   71 LLLSGGAALGTFHVGVVRTLVEHQLLPRVIAGSSVGSIVCAIIATRTDEELQSFFR 126
 
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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