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Conserved domains on  [gi|189095277|ref|NP_001101979|]
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patatin-like phospholipase domain-containing protein 2 [Rattus norvegicus]

Protein Classification

patatin-like phospholipase domain-containing protein; patatin-like phospholipase family protein( domain architecture ID 10163448)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 4-252 0e+00

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: 514.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   4 RETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGP 83
Cdd:cd07220    1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  84 LHPSFNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVR 163
Cdd:cd07220   81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 164 YVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYR 243
Cdd:cd07220  161 YVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYR 240


                 ....*....
gi 189095277 244 DGLRFLRRN 252
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 ...
 4-252 0e+00

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: 514.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   4 RETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGP 83
Cdd:cd07220    1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  84 LHPSFNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVR 163
Cdd:cd07220   81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 164 YVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYR 243
Cdd:cd07220  161 YVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYR 240


                 ....*....
gi 189095277 244 DGLRFLRRN 252
Cdd:cd07220  241 DALRFLKEN 249
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-178 1.94e-22

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: 94.60  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   10 ISFAGCGFLGVYHIGVASCLREHapflVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEA------------- 76
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   77 ----RKRFLGPLHPSFNLVKTIRGCLLKTLPADCHTRASGRLG---------ISLTRVSDGENVIISHFSSKDELIQANV 143
Cdd:pfam01734  77 allrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 189095277  144 CSTFIPVYcgLIPPTLQGVRYVDGGISDNLPLYEL 178
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 3-251 6.77e-17

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 80.33  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   3 PRETKWNISFAGCGFLGVYHIGVASCLREHA-PFlvanaTHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRF- 80
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGiPP-----DVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLs 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  81 -------LGPLHPSFNLVKT--IRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIIShfssKDELIQANVCSTFIPvy 151
Cdd:COG1752   77 lprrllrLDLGLSPGGLLDGdpLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAAIP-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 152 cGLIPP-TLQGVRYVDGGISDNLPLYELKN-----TITVSPFSGESDICP----QDSSTNIHELRITNTSIQFNLRNLYr 221
Cdd:COG1752  151 -GVFPPvEIDGRLYVDGGVVNNLPVDPARAlgadrVIAVDLNPPLRKLPSlldiLGRALEIMFNSILRRELALEPADIL- 228

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 189095277 222 lskaLFPPEPMV-------LREMCKQGYRDGLRFLRR 251
Cdd:COG1752  229 ----IEPDLSGIslldfsrAEELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 4-252 0e+00

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: 514.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   4 RETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGP 83
Cdd:cd07220    1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  84 LHPSFNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVR 163
Cdd:cd07220   81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 164 YVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYR 243
Cdd:cd07220  161 YVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYR 240


                 ....*....
gi 189095277 244 DGLRFLRRN 252
Cdd:cd07220  241 DALRFLKEN 249
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 9-251 1.87e-148

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: 423.30  E-value: 1.87e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   9 NISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSF 88
Cdd:cd07204    1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  89 NLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGG 168
Cdd:cd07204   81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 169 ISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRF 248
Cdd:cd07204  161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                 ...
gi 189095277 249 LRR 251
Cdd:cd07204  241 LER 243
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 9-255 9.85e-121

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: 352.80  E-value: 9.85e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   9 NISFAGCGFLGVYHIGVASCLREHAPFLVANAthIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSF 88
Cdd:cd07218    2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK--ISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  89 NLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGG 168
Cdd:cd07218   80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 169 ISDNLPLYElKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRF 248
Cdd:cd07218  160 FSDNLPTLD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRF 238


                 ....*..
gi 189095277 249 LRRNGLL 255
Cdd:cd07218  239 LHRNNLI 245
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 8-258 6.81e-107

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: 317.87  E-value: 6.81e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   8 WNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPS 87
Cdd:cd07221    1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  88 FNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDG 167
Cdd:cd07221   81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 168 GISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLR 247
Cdd:cd07221  161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                        250
                 ....*....|.
gi 189095277 248 FLRRNGLLNQP 258
Cdd:cd07221  241 FLEENGICNRP 251
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 5-379 1.58e-105

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: 319.93  E-value: 1.58e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   5 ETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPL 84
Cdd:cd07223    7 EGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  85 HPSFNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRY 164
Cdd:cd07223   87 HPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERY 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 165 VDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRD 244
Cdd:cd07223  167 IDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLD 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 245 GLRFLRRNGLLNQPN--PLLALPPVVPQEEDAEEAAVTEERTGGEDRI------------LEHLPARLNEALLEACVEPK 310
Cdd:cd07223  247 ALRFLERRGLTKEPVlwSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWdvpnvlvkdvpnFEQLSPELEAALKKACTRDF 326

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189095277 311 DLMTTLSNMLPVRLATAMMVPYTLPLESAVSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKL 379
Cdd:cd07223  327 STWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQL 395
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 5-267 6.50e-85

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: 266.37  E-value: 6.50e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   5 ETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPL 84
Cdd:cd07219   10 DTPHSISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  85 HPSFNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRY 164
Cdd:cd07219   90 SPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 165 VDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRD 244
Cdd:cd07219  170 IDGGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQD 249

                        250       260
                 ....*....|....*....|....*
gi 189095277 245 GLRFLRRNGL--LNQPNPLLALPPV 267
Cdd:cd07219  250 TVLYLRRLNAvyLNSPSKRVIFPRV 274
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 9-253 1.80e-81

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: 252.64  E-value: 1.80e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   9 NISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGAN-IIEVSKEARKRFLGPLHPS 87
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEfTYKFAEEVRKQRFGAMTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  88 FNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDG 167
Cdd:cd07222   81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 168 GISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLR 247
Cdd:cd07222  161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240


                 ....*.
gi 189095277 248 FLRRNG 253
Cdd:cd07222  241 FLKKEN 246
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 10-186 1.03e-65

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: 209.12  E-value: 1.03e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  10 ISFAGCGFLGVYHIGVASCLREHAPflvaNATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSFN 89
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGP----LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  90 LVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIIShFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGGI 169
Cdd:cd07198   77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                        170
                 ....*....|....*..
gi 189095277 170 SDNLPLYELKNTITVSP 186
Cdd:cd07198  156 SNNLPVAELGNTINVSP 172
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 10-186 4.79e-37

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: 133.31  E-value: 4.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  10 ISFAGCGFLGVYHIGVASCLREHAPFlvANATHIYGASAGALTATALvtgaclgeaganiievskearkrflgpLHPSFN 89
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLL--DCVTYLAGTSGGAWVAATL---------------------------YPPSSS 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  90 LVKTIRGCLLKTLpadchtraSGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPP----------TL 159
Cdd:cd01819   52 LDNKPRQSLEEAL--------SGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKE 123

                        170       180       190
                 ....*....|....*....|....*....|..
gi 189095277 160 QGVRYVDGGISDNLPLY-----ELKNTITVSP 186
Cdd:cd01819  124 KGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 10-251 8.43e-27

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: 107.81  E-value: 8.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  10 ISFAGCGFLGVYHIGVASCL------REHAPFLvanathiyGASAGALTATALVTGACLGEAGANIIEVSKEARKRflgp 83
Cdd:cd07224    2 FSFSAAGLLFPYHLGVLSLLieagviNETTPLA--------GASAGSLAAACSASGLSPEEALEATEELAEDCRSN---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  84 lHPSFNLVKTIRGCLLKTLPADCHTR-ASGRLGISLTRVS---DGENViiSHFSSKDELIQANVCSTFIPVYCGLIPPTL 159
Cdd:cd07224   70 -GTAFRLGGVLRDELDKTLPDDAHERcNRGRIRVAVTQLFpvpRGLLV--SSFDSKSDLIDALLASCNIPGYLAPWPATM 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 160 -QGVRYVDGGISDNLPLYELKN-TITVSPF-SGESDICPQDSSTNIHELritntsiqfnLRNLYR--LSKALFPPEPMVL 234
Cdd:cd07224  147 fRGKLCVDGGFALFIPPTTAADrTVRVCPFpASRSSIKGQNLDNDDTED----------VPYSRRqlLNWALEPADDAML 216

                        250
                 ....*....|....*..
gi 189095277 235 REMCKQGYRDGLRFLRR 251
Cdd:cd07224  217 LELFNEGYKDANEWAKE 233
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-178 1.94e-22

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: 94.60  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   10 ISFAGCGFLGVYHIGVASCLREHapflVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEA------------- 76
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   77 ----RKRFLGPLHPSFNLVKTIRGCLLKTLPADCHTRASGRLG---------ISLTRVSDGENVIISHFSSKDELIQANV 143
Cdd:pfam01734  77 allrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 189095277  144 CSTFIPVYcgLIPPTLQGVRYVDGGISDNLPLYEL 178
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 3-251 6.77e-17

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 80.33  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   3 PRETKWNISFAGCGFLGVYHIGVASCLREHA-PFlvanaTHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRF- 80
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGiPP-----DVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLs 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  81 -------LGPLHPSFNLVKT--IRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIIShfssKDELIQANVCSTFIPvy 151
Cdd:COG1752   77 lprrllrLDLGLSPGGLLDGdpLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAAIP-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 152 cGLIPP-TLQGVRYVDGGISDNLPLYELKN-----TITVSPFSGESDICP----QDSSTNIHELRITNTSIQFNLRNLYr 221
Cdd:COG1752  151 -GVFPPvEIDGRLYVDGGVVNNLPVDPARAlgadrVIAVDLNPPLRKLPSlldiLGRALEIMFNSILRRELALEPADIL- 228

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 189095277 222 lskaLFPPEPMV-------LREMCKQGYRDGLRFLRR 251
Cdd:COG1752  229 ----IEPDLSGIslldfsrAEELIEAGYEAARRALDE 261
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 12-245 9.55e-16

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: 77.26  E-value: 9.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  12 FAGCGFLGVYHIGVASCLREHA--PFlvanaTHIYGASAGALTATALVTGaclgEAGANIIEVSKEAR-KRFLGP----- 83
Cdd:cd07208    3 LEGGGMRGAYTAGVLDAFLEAGirPF-----DLVIGVSAGALNAASYLSG----QRGRALRINTKYATdPRYLGLrsllr 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  84 LHPSFNLVKTIRGCLLKTLPADCHT--RASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGliPPTLQG 161
Cdd:cd07208   74 TGNLFDLDFLYDELPDGLDPFDFEAfaASPARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLFP--PVRIDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277 162 VRYVDGGISDNLPLYEL-------------KNTITVSPFSGESDI-------CPQDSSTNIHELRITNTSIQFnLRNLYR 221
Cdd:cd07208  152 EPYVDGGLSDSIPVDKAiedgadkivviltRPRGYRKKPSKSSPLakllyrkYPNLVEALLRRHSRYNETLEF-IRRLEA 230

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 189095277 222 LSKAL-FPPE-----------PMVLREMCKQGYRDG 245
Cdd:cd07208  231 EGKIFvIAPEkplkvsrlerdPEKLEALYDLGYEDA 266
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
14-175 7.20e-12

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 65.96  E-value: 7.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  14 GCGFLGVYHIGVA-SCLREHAPFlvanaTHIYGASAGALTATALVTGaclgEAGAN---IIEVSKeaRKRFLGPLH---- 85
Cdd:COG4667   12 GGGMRGIFTAGVLdALLEEGIPF-----DLVIGVSAGALNGASYLSR----QPGRArrvITDYAT--DPRFFSLRNflrg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  86 -PSFN---LVKTIRgclLKTLPADCHT-RASGR-LGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGliPPTL 159
Cdd:COG4667   81 gNLFDldfLYDEIP---NELLPFDFETfKASPReFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP--PVEI 155

                        170
                 ....*....|....*.
gi 189095277 160 QGVRYVDGGISDNLPL 175
Cdd:COG4667  156 DGKRYLDGGVADSIPV 171
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 9-176 1.95e-08

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: 54.21  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277   9 NISFAGCGFLGVYHIGVASCLREHaPFLVanaTHIYGASAGALTAtALVtgaCLGEAGANIIEVSKEA-RKRFLGPLHPS 87
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKALEEA-GILK---KRVAGTSAGAITA-ALL---ALGYSAADIKDILKETdFAKLLDSPVGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  88 FNLVKTI--RGCLLK------------------------TLPADCHTRASgrLGISLTRVSDGENVIISHFSSKDELIQA 141
Cdd:cd07207   73 LFLLPSLfkEGGLYKgdaleewlrellkektgnsfatslLRDLDDDLGKD--LKVVATDLTTGALVVFSAETTPDMPVAK 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 189095277 142 NV-CSTFIPVYcgLIPPTLQ-GVRYVDGGISDNLPLY 176
Cdd:cd07207  151 AVrASMSIPFV--FKPVRLAkGDVYVDGGVLDNYPVW 185
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 12-174 3.53e-08

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: 52.93  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  12 FAGCGFLGVYHIGVASCLREHA--PFLVAnathiyGASAGALTAtALVtgaCLGEAGANIIEVSKEARKRFLGPLHPSFN 89
Cdd:cd07205    5 LSGGGARGLAHIGVLKALEEAGipIDIVS------GTSAGAIVG-ALY---AAGYSPEEIEERAKLRSTDLKALSDLTIP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  90 LVKTIRGCLLKTLPAdchtRASGRLGI-SL--------TRVSDGENVIIShfssKDELIQANVCSTFIPvycGLIPP-TL 159
Cdd:cd07205   75 TAGLLRGDKFLELLD----EYFGDRDIeDLwipffivaTDLTSGKLVVFR----SGSLVRAVRASMSIP---GIFPPvKI 143

                        170
                 ....*....|....*
gi 189095277 160 QGVRYVDGGISDNLP 174
Cdd:cd07205  144 DGQLLVDGGVLNNLP 158
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 16-235 1.80e-04

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: 42.72  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  16 GFLGVY-HIGVASCLREHAPFLVanatHIYGASAGALTATALVTGACLGEaganIIE-VSKEARKRFLGPLHPSFNL--- 90
Cdd:cd07210    8 GFFGFYaHLGFLAALLEMGLEPS----AISGTSAGALVGGLFASGISPDE----MAElLLSLERKDFWMFWDPPLRGgll 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  91 -VKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIishFSSKD--ELIQANvcSTFIPVYCgliPPTLQGVRYVDG 167
Cdd:cd07210   80 sGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLL---LSEGDlaEAVAAS--CAVPPLFQ---PVEIGGRPFVDG 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189095277 168 GISDNLPLYEL---------KNTITVSPFSGESDIcpQDSSTNIHELRITNTSIqfnlrNLYRLSKALFPPEPMVLR 235
Cdd:cd07210  152 GVADRLPFDALrpeierilyHHVAPRRPWERLNII--GKISRALIRPFRWNLAI-----LSGVIEDVLEPLGPLLLK 221
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 12-205 3.88e-03

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: 39.12  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  12 FAGCGFLGVYHIGVASCLREHA--PFLVAnathiyGASAGALTATALVTgaclgeaganiievskEARKRFLGPL--HPS 87
Cdd:cd07206   74 LSGGASLGLFHLGVVKALWEQDllPRVIS------GSSAGAIVAALLGT----------------HTDEELIGDLtfQEA 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189095277  88 FNlvKTIRGCLLKTLPADCHTRAsgRLGISLTrvsdGENVIIShfsskdeliQANVCSTFIPvycGLIPPT--------- 158
Cdd:cd07206  132 YE--RTGRIINITVAPAEPHQNS--RLLNALT----SPNVLIW---------SAVLASCAVP---GVFPPVmlmaknrdg 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189095277 159 -----LQGVRYVDGGISDNLPLYELK-----NTITVS-------PF----SGESDICPQDSSTNIHEL 205
Cdd:cd07206  192 eivpyLPGRKWVDGSVSDDLPAKRLArlynvNHFIVSqtnphvvPFlqeySGDITIIPPFSFSNPLKL 259
 
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.
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