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Conserved domains on  [gi|1189406476|gb|ARO50171|]
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patatin-like phospholipase domain containing 2 variant [Homo sapiens]

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 ...
 4-182 2.31e-112

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 cd07220:

Pssm-ID: 416256  Cd Length: 249  Bit Score: 330.17  E-value: 2.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   4 REKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGP 83
Cdd:cd07220     1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  84 LHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV- 162
Cdd:cd07220    81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 163 ---------------------------------------------------------------------VLREMCKQGYR 173
Cdd:cd07220   161 yvdggisdnlpqyelkntitvspfsgesdicprdsstnfhelrftntsiqfnlrnlyrlskalfppepqVLAEMCKQGYR 240


                  ....*....
gi 1189406476 174 DGLRFLQRN 182
Cdd:cd07220   241 DALRFLKEN 249
 
Name Accession Description Interval E-value
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 4-182 2.31e-112

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132859  Cd Length: 249  Bit Score: 330.17  E-value: 2.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   4 REKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGP 83
Cdd:cd07220     1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  84 LHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV- 162
Cdd:cd07220    81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 163 ---------------------------------------------------------------------VLREMCKQGYR 173
Cdd:cd07220   161 yvdggisdnlpqyelkntitvspfsgesdicprdsstnfhelrftntsiqfnlrnlyrlskalfppepqVLAEMCKQGYR 240


                  ....*....
gi 1189406476 174 DGLRFLQRN 182
Cdd:cd07220   241 DALRFLKEN 249
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-151 1.90e-12

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: 65.71  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  10 ISFAGCGFLGVYYVGVASCLREHapflVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEA------------- 76
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  77 ----RKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLG---------ISLTRVSDGENVIISHFNSKDELIQANV 143
Cdd:pfam01734  77 allrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvISTALGTRARILLPDDLDDDEDLADAVL 156


                  ....*...
gi 1189406476 144 CSGFIPVY 151
Cdd:pfam01734 157 ASSALPGV 164
 
Name Accession Description Interval E-value
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 4-182 2.31e-112

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132859  Cd Length: 249  Bit Score: 330.17  E-value: 2.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   4 REKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGP 83
Cdd:cd07220     1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  84 LHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV- 162
Cdd:cd07220    81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 163 ---------------------------------------------------------------------VLREMCKQGYR 173
Cdd:cd07220   161 yvdggisdnlpqyelkntitvspfsgesdicprdsstnfhelrftntsiqfnlrnlyrlskalfppepqVLAEMCKQGYR 240


                  ....*....
gi 1189406476 174 DGLRFLQRN 182
Cdd:cd07220   241 DALRFLKEN 249
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 9-181 4.14e-92

Patatin-like phospholipase domain containing protein family; Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity.


Pssm-ID: 132843 [Multi-domain]  Cd Length: 243  Bit Score: 278.08  E-value: 4.14e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSF 88
Cdd:cd07204     1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  89 NLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV------ 162
Cdd:cd07204    81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVryidgg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 163 ----------------------------------------------------------------VLREMCKQGYRDGLRF 178
Cdd:cd07204   161 lsdnlpilddentitvspfsgesdicpqdkssnllevniantsiqlslenlyrlnralfppsleILSRMCQQGYLDALRF 240


                  ...
gi 1189406476 179 LQR 181
Cdd:cd07204   241 LER 243
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 9-185 8.08e-66

Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity.


Pssm-ID: 132857  Cd Length: 245  Bit Score: 210.66  E-value: 8.08e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANAthIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSF 88
Cdd:cd07218     2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK--ISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  89 NLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV------ 162
Cdd:cd07218    80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVrymdgg 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 163 ---------------------------------------------------------------VLREMCKQGYRDGLRFL 179
Cdd:cd07218   160 fsdnlptldentitvspfcgesdicprdnssqlfhinwantsielsrqniyrlvrilfpprpeVLSSLCQQGFDDALRFL 239


                  ....*.
gi 1189406476 180 QRNGLL 185
Cdd:cd07218   240 HRNNLI 245
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 8-188 3.42e-62

Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes and is an indicator of the nutritional state. PNPLA3 is also known as adiponutrin (ADPN) or iPLA2-epsilon. Human adiponutrins are bound to the cell membrane of adipocytes and show transacylase, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: ADPN (adiponutrin) from mammals, PNPLA3 (Patatin-like phospholipase domain-containing protein 3), and iPLA2-epsilon (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132860  Cd Length: 252  Bit Score: 201.54  E-value: 3.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   8 WNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPS 87
Cdd:cd07221     1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  88 FNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV----- 162
Cdd:cd07221    81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVryvdg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 163 -----------------------------------------------------------------VLREMCKQGYRDGLR 177
Cdd:cd07221   161 gvsdnvpffdakttitvspfygeydicpkvkstnflhvdftklslrlctenlylltralfppdvkVLGEICLRGYLDAFR 240

                         250
                  ....*....|.
gi 1189406476 178 FLQRNGLLNRP 188
Cdd:cd07221   241 FLEENGICNRP 251
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 5-317 1.80e-60

Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), plays a role in regulation of adipocyte differentiation. PNPLA5 is expressed in brain tissue in high mRNA levels and low levels in liver tissue. There is no concrete evidence in support of the enzymatic activity of GS2L. This family includes patatin-like proteins: GS2L (GS2-like) and PNPLA5 (Patatin-like phospholipase domain-containing protein 5) reported exclusively in mammals.


Pssm-ID: 132862  Cd Length: 405  Bit Score: 202.06  E-value: 1.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   5 EKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPL 84
Cdd:cd07223     7 EGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  85 HPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV-- 162
Cdd:cd07223    87 HPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGEry 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 163 --------------------------------------------------------------------VLREMCKQGYRD 174
Cdd:cd07223   167 idgalsnnlpfsdcpstitvspfhgtvdicpqstsanlhelnafnasfqistrnfflglkclippkpeVVADNCRQGYLD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476 175 GLRFLQRNGLLNRPnPLLAL----PPARPHGPEDK--DQAVESAQAEDYSqLPgedHIL-------EHLPARLNEALLEA 241
Cdd:cd07223   247 ALRFLERRGLTKEP-VLWSLvskePPAPADGPRDTghDQGQKGGLSLNWD-VP---NVLvkdvpnfEQLSPELEAALKKA 321

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189406476 242 CVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGR 317
Cdd:cd07223   322 CTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLR 397
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 10-162 7.49e-55

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: 179.84  E-value: 7.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  10 ISFAGCGFLGVYYVGVASCLREHAPflvaNATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSFN 89
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGP----LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189406476  90 LVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIIShFNSKDELIQANVCSGFIPVYCGLIPPSLQGV 162
Cdd:cd07198    77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGR 148
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 9-162 2.73e-51

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 177.39  E-value: 2.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSF 88
Cdd:cd07219    14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189406476  89 NLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGV 162
Cdd:cd07219    94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGV 167
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 9-161 6.58e-40

Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene sequence-2), shows both lipase and transacylation activities. GS2 lipase is expressed in various tissues, predominantly in muscle and adipocytes tissue. It is also expressed in keratinocytes and shows retinyl ester hydrolase, acylglycerol, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: GS2 from mammals, PNPLA4 (Patatin-like phospholipase domain-containing protein 4), and iPLA2-eta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132861 [Multi-domain]  Cd Length: 246  Bit Score: 143.24  E-value: 6.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFI-EVSKEARKRFLGPLHPS 87
Cdd:cd07222     1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTyKFAEEVRKQRFGAMTPG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189406476  88 FNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQG 161
Cdd:cd07222    81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKG 154
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 10-157 5.93e-31

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: 116.36  E-value: 5.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  10 ISFAGCGFLGVYYVGVASCLREHAPFlvANATHIYGASAGALTATALvtgvclgeagakfievskearkrflgpLHPSFN 89
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLL--DCVTYLAGTSGGAWVAATL---------------------------YPPSSS 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189406476  90 LVKIIRSFLLkvlpadshEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPP 157
Cdd:cd01819    52 LDNKPRQSLE--------EALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPP 111
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 10-153 9.47e-19

Patatin-like phospholipase; 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: 132863  Cd Length: 233  Bit Score: 84.70  E-value: 9.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  10 ISFAGCGFLGVYYVGVASCL------REHAPFLvanathiyGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRflgp 83
Cdd:cd07224     2 FSFSAAGLLFPYHLGVLSLLieagviNETTPLA--------GASAGSLAAACSASGLSPEEALEATEELAEDCRSN---- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189406476  84 lHPSFNLVKIIRSFLLKVLPADSHEH-ASGRLGISLTRVS---DGENViiSHFNSKDELIQANVCSGFIPVYCG 153
Cdd:cd07224    70 -GTAFRLGGVLRDELDKTLPDDAHERcNRGRIRVAVTQLFpvpRGLLV--SSFDSKSDLIDALLASCNIPGYLA 140
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-151 1.90e-12

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: 65.71  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  10 ISFAGCGFLGVYYVGVASCLREHapflVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEA------------- 76
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  77 ----RKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLG---------ISLTRVSDGENVIISHFNSKDELIQANV 143
Cdd:pfam01734  77 allrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvISTALGTRARILLPDDLDDDEDLADAVL 156


                  ....*...
gi 1189406476 144 CSGFIPVY 151
Cdd:pfam01734 157 ASSALPGV 164
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 12-162 3.32e-04

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: 42.21  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  12 FAGCGFLGVYYVGVASCLREHA--PFlvanaTHIYGASAGALTATALVTGvclGEAGAKFIEVSKEARKRFLGP-----L 84
Cdd:cd07208     3 LEGGGMRGAYTAGVLDAFLEAGirPF-----DLVIGVSAGALNAASYLSG---QRGRALRINTKYATDPRYLGLrsllrT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  85 HPSFNLVKIIRSFLLKVLPADSH---EHAsGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGliPPSLQG 161
Cdd:cd07208    75 GNLFDLDFLYDELPDGLDPFDFEafaASP-ARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLFP--PVRIDG 151


                  .
gi 1189406476 162 V 162
Cdd:cd07208   152 E 152
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 9-151 7.84e-04

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: 40.34  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476   9 NISFAGCGFLGVYYVGVASCLREHaPFLVanaTHIYGASAGALTAtALvtgVCLGEAGAKFIEVSKEA-RKRFLGPLHPS 87
Cdd:cd07207     1 NLVFEGGGAKGIAYIGALKALEEA-GILK---KRVAGTSAGAITA-AL---LALGYSAADIKDILKETdFAKLLDSPVGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189406476  88 -FNLVKIIRSFLL-----------------------KVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANV 143
Cdd:cd07207    73 lFLLPSLFKEGGLykgdaleewlrellkektgnsfaTSLLRDLDDDLGKDLKVVATDLTTGALVVFSAETTPDMPVAKAV 152


                  ....*....
gi 1189406476 144 -CSGFIPVY 151
Cdd:cd07207   153 rASMSIPFV 161
 
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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