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Conserved domains on  [gi|498257647|ref|WP_010571803|]
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patatin-like phospholipase RssA [Leptospira broomii]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Patatin_and_cPLA2 super family cl11396
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 6-295 8.56e-102

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


The actual alignment was detected with superfamily member PRK10279:

Pssm-ID: 416256 [Multi-domain]  Cd Length: 300  Bit Score: 300.09  E-value: 8.56e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   6 KRRIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMDWTFG-GG 84
Cdd:PRK10279   3 KIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQrGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  85 LIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPV 164
Cdd:PRK10279  83 LLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647 165 PVSLCRAMGADYVIAVDL-------NQDLLEKREAEDkKEISIEPMSrwrswtskfWGSDLDEHL----KAEKDDKPGIM 233
Cdd:PRK10279 163 PVSLTRALGADIVIAVDLqhdahlmQQDLLSFNVSEE-NSENGDSLP---------WHARLKERLgsitTRRAVTAPTAM 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498257647 234 EVVSKSINIMQIRITRSRMAGDPPDILLAPRLRYIGLMEFHRGKEAIAEGRDIVRKMAPALI 295
Cdd:PRK10279 233 EIMTTSIQVLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQLAVEKKMDELL 294
 
Name Accession Description Interval E-value
PRK10279 PRK10279
patatin-like phospholipase RssA;
6-295 8.56e-102

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 300.09  E-value: 8.56e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   6 KRRIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMDWTFG-GG 84
Cdd:PRK10279   3 KIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQrGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  85 LIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPV 164
Cdd:PRK10279  83 LLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647 165 PVSLCRAMGADYVIAVDL-------NQDLLEKREAEDkKEISIEPMSrwrswtskfWGSDLDEHL----KAEKDDKPGIM 233
Cdd:PRK10279 163 PVSLTRALGADIVIAVDLqhdahlmQQDLLSFNVSEE-NSENGDSLP---------WHARLKERLgsitTRRAVTAPTAM 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498257647 234 EVVSKSINIMQIRITRSRMAGDPPDILLAPRLRYIGLMEFHRGKEAIAEGRDIVRKMAPALI 295
Cdd:PRK10279 233 EIMTTSIQVLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQLAVEKKMDELL 294
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 6-293 2.86e-87

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 261.38  E-value: 2.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   6 KRRIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAG-KLHALESWVESLEWKDILG--------- 75
Cdd:COG1752    4 RPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGySADELEELWRSLDRRDLFDlslprrllr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  76 FMDWTFGGGLIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWL 155
Cdd:COG1752   84 LDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647 156 VDGGLVNPVPVSLCRAMGADYVIAVDLNQDLlekreaedkkeisiepmsrwrswtskfwgsdldehlkaekDDKPGIMEV 235
Cdd:COG1752  164 VDGGVVNNLPVDPARALGADRVIAVDLNPPL----------------------------------------RKLPSLLDI 203

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498257647 236 VSKSINIMQIRITRSRMAGDPPDILLAPRLRYIGLMEFHRGKEAIAEGRDIVRKMAPA 293
Cdd:COG1752  204 LGRALEIMFNSILRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 9-182 7.35e-79

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: 236.79  E-value: 7.35e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   9 IGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMDWTF-GGGLIR 87
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVLRLLDLSAsRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  88 GKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPVPVS 167
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 498257647 168 LCRAMGADYVIAVDL 182
Cdd:cd07228  161 VARALGADIVIAVDL 175
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 11-166 1.41e-26

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: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   11 LALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHA-LESWVESLEWKDILGFMDWT--------- 80
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEeIEDLLLELDLNLFLSLIRKRalsllallr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   81 ---FGGGLIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEV-----------------WIREGSIFEAVRASIS 140
Cdd:pfam01734  81 gliGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTvistalgtrarillpddLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*.
gi 498257647  141 LPGIFTPVLKDGRWLVDGGLVNPVPV 166
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPV 186
 
Name Accession Description Interval E-value
PRK10279 PRK10279
patatin-like phospholipase RssA;
6-295 8.56e-102

patatin-like phospholipase RssA;


Pssm-ID: 182352 [Multi-domain]  Cd Length: 300  Bit Score: 300.09  E-value: 8.56e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   6 KRRIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMDWTFG-GG 84
Cdd:PRK10279   3 KIKIGLALGSGAARGWSHIGVINALKKVGIEIDIVAGCSIGSLVGAAYACDRLSALEDWVTSFSYWDVLRLMDLSWQrGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  85 LIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPV 164
Cdd:PRK10279  83 LLRGERVFNQYREIMPETEIENCSRRFGAVATNLSTGRELWFTEGDLHLAIRASCSMPGLMAPVAHNGYWLVDGAVVNPV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647 165 PVSLCRAMGADYVIAVDL-------NQDLLEKREAEDkKEISIEPMSrwrswtskfWGSDLDEHL----KAEKDDKPGIM 233
Cdd:PRK10279 163 PVSLTRALGADIVIAVDLqhdahlmQQDLLSFNVSEE-NSENGDSLP---------WHARLKERLgsitTRRAVTAPTAM 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498257647 234 EVVSKSINIMQIRITRSRMAGDPPDILLAPRLRYIGLMEFHRGKEAIAEGRDIVRKMAPALI 295
Cdd:PRK10279 233 EIMTTSIQVLENRLKRNRMAGDPPDILIQPVCPQISTLDFHRAHAAIAAGQLAVEKKMDELL 294
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 6-293 2.86e-87

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 261.38  E-value: 2.86e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   6 KRRIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAG-KLHALESWVESLEWKDILG--------- 75
Cdd:COG1752    4 RPKIGLVLSGGGARGAAHIGVLKALEEAGIPPDVIAGTSAGAIVGALYAAGySADELEELWRSLDRRDLFDlslprrllr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  76 FMDWTFGGGLIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWL 155
Cdd:COG1752   84 LDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGPLADAVRASAAIPGVFPPVEIDGRLY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647 156 VDGGLVNPVPVSLCRAMGADYVIAVDLNQDLlekreaedkkeisiepmsrwrswtskfwgsdldehlkaekDDKPGIMEV 235
Cdd:COG1752  164 VDGGVVNNLPVDPARALGADRVIAVDLNPPL----------------------------------------RKLPSLLDI 203

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498257647 236 VSKSINIMQIRITRSRMAGDPPDILLAPRLRYIGLMEFHRGKEAIAEGRDIVRKMAPA 293
Cdd:COG1752  204 LGRALEIMFNSILRRELALEPADILIEPDLSGISLLDFSRAEELIEAGYEAARRALDE 261
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 9-182 7.35e-79

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: 236.79  E-value: 7.35e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   9 IGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMDWTF-GGGLIR 87
Cdd:cd07228    1 IGLALGSGGARGWAHIGVLRALEEEGIEIDIIAGSSIGALVGALYAAGHLDALEEWVRSLSQRDVLRLLDLSAsRSGLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  88 GKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPVPVS 167
Cdd:cd07228   81 GEKVLEYLREIMGGVTIEELPIPFAAVATDLQTGKEVWFREGSLIDAIRASISIPGIFAPVEHNGRLLVDGGVVNPIPVS 160

                        170
                 ....*....|....*
gi 498257647 168 LCRAMGADYVIAVDL 182
Cdd:cd07228  161 VARALGADIVIAVDL 175
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 9-182 1.64e-63

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: 197.77  E-value: 1.64e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   9 IGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMDWTF-GGGLIR 87
Cdd:cd07205    1 IGLALSGGGARGLAHIGVLKALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKALSDLTIpTAGLLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  88 GKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPVPVS 167
Cdd:cd07205   81 GDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGSLVRAVRASMSIPGIFPPVKIDGQLLVDGGVLNNLPVD 160

                        170
                 ....*....|....*
gi 498257647 168 LCRAMGADYVIAVDL 182
Cdd:cd07205  161 VLRELGADIIIAVDL 175
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 11-219 1.48e-32

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: 119.32  E-value: 1.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  11 LALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALEsWVESLeWKDIlgfmdwTFGGGLIRG-- 88
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEPDIISGTSIGAINGALIAGGDPEAVE-RLEKL-WREL------SREDVFLRGll 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  89 KKLFDFFAQEFRDAEIHELTlpygAVAADLDTGVEVWIRE---GSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPVP 165
Cdd:cd07209   73 DRALDFDTLRLLAILFAGLV----IVAVNVLTGEPVYFDDipdGILPEHLLASAALPPFFPPVEIDGRYYWDGGVVDNTP 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498257647 166 VSLCRAMGADYVIAVDLNQDLLEKREaedkkeiSIEPMSRWRSWTSKFWGSDLD 219
Cdd:cd07209  149 LSPAIDLGADEIIVVSLSDKGRDDRK-------GTPPTTLIEILPRLFLRSGLD 195
Pat_PNPLA6_PNPLA7 cd07225
Patatin-like phospholipase domain containing protein 6 and protein 7; Patatin-like ...
 8-220 5.17e-32

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: 120.58  E-value: 5.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   8 RIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAG------KLHALEsWVESLE--WKDILgfmDW 79
Cdd:cd07225   15 SIALVLGGGGARGCAHIGVIKALEEAGIPVDMVGGTSIGAFIGALYAEErnisrmKQRARE-WAKDMTsiWKKLL---DL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  80 TFG-GGLIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVL--KDGRWLV 156
Cdd:cd07225   91 TYPiTSMFSGAAFNRSIHSIFGDKQIEDLWLPYFTITTDITASAMRVHTDGSLWRYVRASMSLSGYLPPLCdpKDGHLLM 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498257647 157 DGGLVNPVPVSLCRAMGADYVIAVDLNqdllekreAEDKKEISI--EPMS-------RWRSWTSKFWGSDLDE 220
Cdd:cd07225  171 DGGYINNLPADVARSMGAKTVIAIDVG--------SQDETDLTNygDALSgwwllwkRWNPLAEKVKVPNMAE 235
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 9-167 4.86e-31

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: 115.52  E-value: 4.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   9 IGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGK-LHALESWVESLEWKDILGFMDWTFGGGLIR 87
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMGLEPSAISGTSAGALVGGLFASGIsPDEMAELLLSLERKDFWMFWDPPLRGGLLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  88 GKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKDGRWLVDGGLVNPVPVS 167
Cdd:cd07210   81 GDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGDLAEAVAASCAVPPLFQPVEIGGRPFVDGGVADRLPFD 160
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 11-172 1.09e-28

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: 108.20  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  11 LALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMDWTF-GGGLIRGk 89
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPLIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFpPTGRLLG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  90 KLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWI---REGSIFEAVRASISLPGIFTPV--LKDGRWLVDGGLVNPV 164
Cdd:cd07198   80 ILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVsdtSKGELWSAVRASSSIPGYFGPVplSFRGRRYGDGGLSNNL 159


                 ....*...
gi 498257647 165 PVSLCRAM 172
Cdd:cd07198  160 PVAELGNT 167
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 11-166 1.41e-26

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: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   11 LALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHA-LESWVESLEWKDILGFMDWT--------- 80
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRFDVISGTSAGAINAALLALGRDPEeIEDLLLELDLNLFLSLIRKRalsllallr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   81 ---FGGGLIRGKKLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEV-----------------WIREGSIFEAVRASIS 140
Cdd:pfam01734  81 gliGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTvistalgtrarillpddLDDDEDLADAVLASSA 160

                         170       180
                  ....*....|....*....|....*.
gi 498257647  141 LPGIFTPVLKDGRWLVDGGLVNPVPV 166
Cdd:pfam01734 161 LPGVFPPVRLDGELYVDGGLVDNVPV 186
Pat_Fungal_NTE1 cd07227
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ...
 7-182 2.56e-26

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: 104.50  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   7 RRIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYS---------------AGKLHALESWVESLEWK 71
Cdd:cd07227    9 QAIGLVLGGGGARGISHIGILQALEEAGIPIDAIGGTSIGSFVGGLYAreadlvpifgrakkfAGRMASMWRFLSDVTYP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  72 dilgFMDWTFGGGLIRGkklfdfFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSIFEAVRASISLPGIFTPVLKD 151
Cdd:cd07227   89 ----FASYTTGHEFNRG------IWKTFGNTHIEDFWIPFYANSTNITHSRMEIHSSGYAWRYIRASMSLAGLLPPLSDN 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 498257647 152 GRWLVDGGLVNPVPVSLCRAMGADYVIAVDL 182
Cdd:cd07227  159 GSMLLDGGYMDNLPVSPMRSLGIRDIFAVDV 189
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 11-180 2.11e-22

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: 93.83  E-value: 2.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  11 LALGSGSARGWSHIGVIQELENLGIRP-DIVCGTSIGSLVGAFYSAGKL-HALESWVESLEWKDILGFMDWTFGGGLIRG 88
Cdd:cd07208    1 LVLEGGGMRGAYTAGVLDAFLEAGIRPfDLVIGVSAGALNAASYLSGQRgRALRINTKYATDPRYLGLRSLLRTGNLFDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  89 KKLFD---FFAQEFRDAEIHELTLPYGAVAADLDTGVEVWIREGSI----FEAVRASISLPGIFTPVLKDGRWLVDGGLV 161
Cdd:cd07208   81 DFLYDelpDGLDPFDFEAFAASPARFYVVATDADTGEAVYFDKPDIlddlLDALRASSALPGLFPPVRIDGEPYVDGGLS 160

                        170
                 ....*....|....*....
gi 498257647 162 NPVPVSLCRAMGADYVIAV 180
Cdd:cd07208  161 DSIPVDKAIEDGADKIVVI 179
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 11-168 6.56e-22

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: 90.80  E-value: 6.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  11 LALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAF----YSAGKLHALeswvesLEWKDILGFMDWTFG---- 82
Cdd:cd07207    2 LVFEGGGAKGIAYIGALKALEEAGILKKRVAGTSAGAITAALlalgYSAADIKDI------LKETDFAKLLDSPVGllfl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  83 -------GGLIRGKKLFDFFAQEFRDAEIHELTLPYGA------------VAADLDTGVEVWI-----REGSIFEAVRAS 138
Cdd:cd07207   76 lpslfkeGGLYKGDALEEWLRELLKEKTGNSFATSLLRdldddlgkdlkvVATDLTTGALVVFsaettPDMPVAKAVRAS 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 498257647 139 ISLPGIFTPV-LKDGRWLVDGGLVNPVPVSL 168
Cdd:cd07207  156 MSIPFVFKPVrLAKGDVYVDGGVLDNYPVWL 186
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
8-207 1.31e-21

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 91.76  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   8 RIGLALGSGSARGwshI---GVIQELENLGIRPDIVCGTSIGSLVGAFYSAG-KLHALESWVESLEWKDilgFMDWtfgG 83
Cdd:COG4667    5 KTALVLEGGGMRG---IftaGVLDALLEEGIPFDLVIGVSAGALNGASYLSRqPGRARRVITDYATDPR---FFSL---R 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  84 GLIRGKKLFDF-FAqeFRDAEIHELTLPYGA----------VAADLDTGVEVWIR----EGSIFEAVRASISLPGIFTPV 148
Cdd:COG4667   76 NFLRGGNLFDLdFL--YDEIPNELLPFDFETfkasprefyvVATNADTGEAEYFSkkddDYDLLDALRASSALPLLYPPV 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498257647 149 LKDGRWLVDGGLVNPVPVSLCRAMGADYVIAVdlnqdlLEKREAEDKKEISIEPMSRWR 207
Cdd:COG4667  154 EIDGKRYLDGGVADSIPVREAIRDGADKIVVI------LTRPRGYRKKPSKFKRLLRRL 206
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 1-164 6.69e-07

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


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 49.90  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   1 MGNNGKRRIgLALGSGSARGWSHIGVIQELE-NLGIRP----DIVCGTSIGSLVGAFYSAGKL--HALESWVEslEWKDI 73
Cdd:COG3621    1 MSANKPFRI-LSLDGGGIRGLIPARILAELEeRLGKPLaeyfDLIAGTSTGGIIALGLAAGYSaeEILDLYEE--EGKEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  74 ---LGFMDWTFGGGLIRGK----KLFDFFAQEFRDAEIHELTLPYGAVAADLDTGVEVWI--------REGSIF--EAVR 136
Cdd:COG3621   78 fpkSRWRKLLSLRGLFGPKydseGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFksphakfdRDRDFLlvDVAR 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 498257647 137 ASISLPGIFTPV-----LKDGRWLVDGGLV--NPV 164
Cdd:COG3621  158 ATSAAPTYFPPAqiknlTGEGYALIDGGVFanNPA 192
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 11-179 2.39e-06

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: 46.64  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  11 LALGSGSARGWSHIGVIQELENLGIR--PDIVCGTSIGSLVGAFYS--AGKLHALESWVESLEWKDILGFmdwtfgggli 86
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLLdcVTYLAGTSGGAWVAATLYppSSSLDNKPRQSLEEALSGKLWV---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  87 rgkklfdffaqefrdaEIHELTLPYGAVAADLDTGVEVWiregsifEAVRASISLPGIFTPVL------------KDGRW 154
Cdd:cd01819   71 ----------------SFTPVTAGENVLVSRFVSKEELI-------RALFASGSWPSYFGLIPpaelytsksnlkEKGVR 127

                        170       180
                 ....*....|....*....|....*..
gi 498257647 155 LVDGGLVN--PVPVSLCRAMGADYVIA 179
Cdd:cd01819  128 LVDGGVSNnlPAPVLLRPGRGVTLTIS 154
Pat_TGL4-5_like cd07230
Triacylglycerol lipase 4 and 5; TGL4 and TGL5 are triacylglycerol lipases that are involved in ...
 8-213 7.67e-06

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: 46.83  E-value: 7.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   8 RIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAFYSAGKLHALESWVESLEWKDILGFMD--------- 78
Cdd:cd07230   73 RTALLLSGGGTFGMFHIGVLKALFEANLLPRIISGSSAGSIVAAILCTHTDEEIPELLEEFPYGDFNVFEDpdqeenvlq 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  79 --------WTF--GGGLIRGKKLF--DFFAQEFRD------------AEIHELT--LPYgaVAAdldTGVEVWiregsif 132
Cdd:cd07230  153 klsrflkyGSWfdISHLTRVMRGFlgDLTFQEAYNrtrrilnitvspASIYELPrlLNY--ITA---PNVLIW------- 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647 133 EAVRASISLPGIF--TPVL-KD-------------GRWlVDGGLVNPVPVS-LCRAMGADYVIAVDLNQD---LLEKREA 192
Cdd:cd07230  221 SAVCASCSVPGVFpsSPLYeKDpktgeivpwnpssVKW-IDGSVDNDLPMTrLSEMFNVNHFIVSQVNPHvvpFLKKSES 299

                        250       260
                 ....*....|....*....|.
gi 498257647 193 EDKKEISIEPMSRWRSWTSKF 213
Cdd:cd07230  300 CVGGEVEDELSARFKRWLNNV 320
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 11-164 1.67e-05

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: 45.40  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  11 LALGSGSARGWSHIGVIQELEN-LGIRP------DIVCGTSIGSLVGAFYSAGKLHAleswveslewKDILGFMdwtfgg 83
Cdd:cd07199    2 LSLDGGGIRGIIPAEILAELEKrLGKPSriadlfDLIAGTSTGGIIALGLALGRYSA----------EELVELY------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  84 gLIRGKKLFDFFA-QEFRDAEIHELTLP-YGAVAADLDTGVEVWiregsifEAVRASISLPGIFTPV----LKDGRWLVD 157
Cdd:cd07199   66 -EELGRKIFPRVLvTAYDLSTGKPVVFSnYDAEEPDDDDDFKLW-------DVARATSAAPTYFPPAviesGGDEGAFVD 137


                 ....*....
gi 498257647 158 GGLV--NPV 164
Cdd:cd07199  138 GGVAanNPA 146
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 8-52 4.76e-04

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: 41.48  E-value: 4.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 498257647   8 RIGLALGSGSARGWSHIGVIQELENLGIRPDIVCGTSIGSLVGAF 52
Cdd:cd07232   67 RTALCLSGGAAFAYYHFGVVKALLDADLLPNVISGTSGGSLVAAL 111
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 6-184 8.94e-04

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 40.35  E-value: 8.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647   6 KRRIgLALGSGSARGWSHIGVIQELE----NLGIRPDIVCGTSIGSLVGAFYSAGK--LHALESWVESLEW---KDILGF 76
Cdd:cd07213    1 KYRI-LSLDGGGVKGIVQLVLLKRLAeefpSFLDQIDLFAGTSAGSLIALGLALGYspRQVLKLYEEVGLKvfsKSSAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498257647  77 MdwTFGGGLIRGKKLFDFFAQEFRDAEIHELTlPYGAVAA-DLDTGVEVWIR----------------EGSIFEAVRASI 139
Cdd:cd07213   80 G--AGNNQYFAAGFLKAFAEVFFGDLTLGDLK-RKVLVPSfQLDSGKDDPNRrwkpklfhnfpgepdlDELLVDVCLRSS 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 498257647 140 SLPGIFTPVlkDGrwLVDGGLV--NPVPVSLCRAMGAdYVIAVDLNQ 184
Cdd:cd07213  157 AAPTYFPSY--QG--YVDGGVFanNPSLCAIAQAIGE-EGLNIDLKD 198
 
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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