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Conserved domains on  [gi|20304127|ref|NP_620169|]
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patatin-like phospholipase domain-containing protein 5 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 1-405 0e+00

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: 852.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127   1 MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLER 80
Cdd:cd07223   1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  81 LSLSILHPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPE 160
Cdd:cd07223  81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 161 FRGERYIDGALSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNC 240
Cdd:cd07223 161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 241 RQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKK 320
Cdd:cd07223 241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 321 ACTRDPSRWARFWHSGPGQVLTYLLLPCTLPFEYIYFRSRRLVVWLPDVPADLWWMQGLLRNMALEVFSRTKAQLLGPIS 400
Cdd:cd07223 321 ACTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                ....*
gi 20304127 401 PPATR 405
Cdd:cd07223 401 PPVTR 405
 
Name Accession Description Interval E-value
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 1-405 0e+00

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: 852.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127   1 MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLER 80
Cdd:cd07223   1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  81 LSLSILHPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPE 160
Cdd:cd07223  81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 161 FRGERYIDGALSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNC 240
Cdd:cd07223 161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 241 RQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKK 320
Cdd:cd07223 241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 321 ACTRDPSRWARFWHSGPGQVLTYLLLPCTLPFEYIYFRSRRLVVWLPDVPADLWWMQGLLRNMALEVFSRTKAQLLGPIS 400
Cdd:cd07223 321 ACTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                ....*
gi 20304127 401 PPATR 405
Cdd:cd07223 401 PPVTR 405
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 12-177 4.33e-17

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: 79.19  E-value: 4.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127    12 LSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVD-------------FCCSHLLGMVGQL 78
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDPEeiedllleldlnlFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127    79 ERLSLSILHPAYAPIEHVKQQLQDALPPD-------------AHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALV 145
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLtleelaarlslllVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 20304127   146 CTLYFPFYcgLIPPEFRGERYIDGALSNNLPF 177
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 9-253 2.66e-11

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 63.77  E-value: 2.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127   9 RWNLSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGM----------VGQL 78
Cdd:COG1752   6 KIGLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSADELEELWRSLdrrdlfdlslPRRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  79 ERLSLSILHPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDfatcDELIQALVCTLYFPfycGLIP 158
Cdd:COG1752  82 LRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDS----GPLADAVRASAAIP---GVFP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 159 P-EFRGERYIDGALSNNLPF-----ADCPSTITVSPFHgtvdicPQSTSPNLHEL--NVFNFSFQISTENFFLGLIC--L 228
Cdd:COG1752 155 PvEIDGRLYVDGGVVNNLPVdparaLGADRVIAVDLNP------PLRKLPSLLDIlgRALEIMFNSILRRELALEPAdiL 228

                       250       260       270
                ....*....|....*....|....*....|...
gi 20304127 229 IPPSL--------EVVADNCRQGYLDALRFLER 253
Cdd:COG1752 229 IEPDLsgislldfSRAEELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 1-405 0e+00

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: 852.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127   1 MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLER 80
Cdd:cd07223   1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  81 LSLSILHPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPE 160
Cdd:cd07223  81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 161 FRGERYIDGALSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNC 240
Cdd:cd07223 161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 241 RQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKK 320
Cdd:cd07223 241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 321 ACTRDPSRWARFWHSGPGQVLTYLLLPCTLPFEYIYFRSRRLVVWLPDVPADLWWMQGLLRNMALEVFSRTKAQLLGPIS 400
Cdd:cd07223 321 ACTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                ....*
gi 20304127 401 PPATR 405
Cdd:cd07223 401 PPVTR 405
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 11-253 1.91e-144

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: 411.36  E-value: 1.91e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPAY 90
Cdd:cd07204   1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  91 APIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDGA 170
Cdd:cd07204  81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 171 LSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRF 250
Cdd:cd07204 161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                ...
gi 20304127 251 LER 253
Cdd:cd07204 241 LER 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 7-253 3.86e-99

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: 296.27  E-value: 3.86e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127   7 EGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSIL 86
Cdd:cd07220   2 DSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  87 HPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERY 166
Cdd:cd07220  82 HPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRY 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 167 IDGALSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLD 246
Cdd:cd07220 162 VDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRD 241


                ....*..
gi 20304127 247 ALRFLER 253
Cdd:cd07220 242 ALRFLKE 248
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 10-260 7.33e-92

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: 277.81  E-value: 7.33e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  10 WNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPA 89
Cdd:cd07221   1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  90 YAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDG 169
Cdd:cd07221  81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 170 ALSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALR 249
Cdd:cd07221 161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                       250
                ....*....|.
gi 20304127 250 FLERRGLTKEP 260
Cdd:cd07221 241 FLEENGICNRP 251
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 11-256 4.41e-84

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: 257.66  E-value: 4.41e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQgaRRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPAY 90
Cdd:cd07218   2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLL--NKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  91 APIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDGA 170
Cdd:cd07218  80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 171 LSNNLPFADcPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRF 250
Cdd:cd07218 160 FSDNLPTLD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRF 238


                ....*.
gi 20304127 251 LERRGL 256
Cdd:cd07218 239 LHRNNL 244
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 12-188 1.02e-63

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: 202.57  E-value: 1.02e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  12 LSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPAYA 91
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  92 PIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTdFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDGAL 171
Cdd:cd07198  77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                       170
                ....*....|....*..
gi 20304127 172 SNNLPFADCPSTITVSP 188
Cdd:cd07198 156 SNNLPVAELGNTINVSP 172
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 11-253 5.43e-62

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: 205.13  E-value: 5.43e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPAY 90
Cdd:cd07219  14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  91 APIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDGA 170
Cdd:cd07219  94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 171 LSNNLPFADCPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRF 250
Cdd:cd07219 174 FTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLY 253


                ...
gi 20304127 251 LER 253
Cdd:cd07219 254 LRR 256
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 11-255 9.92e-57

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: 187.15  E-value: 9.92e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNA-VSIVCGKSVDFCCSHLLGMVGQLERLSLSILHPA 89
Cdd:cd07222   1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAaVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  90 YAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPPEFRGERYIDG 169
Cdd:cd07222  81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 170 ALSNNLPFADCPSTITVSPFHGTVDICPQS-TSPNLHeLNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDAL 248
Cdd:cd07222 161 GFTNSLPVLPVGRTITVSPFSGRADICPQDkGQLDLY-VRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                ....*..
gi 20304127 249 RFLERRG 255
Cdd:cd07222 240 RFLKKEN 246
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 13-189 1.89e-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: 86.62  E-value: 1.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  13 SFSGAGYLGAHHVGATECLrQRAPRLLQGARrIYGSSSGALNAVSIVCGKSVDFC---CSHLL------GMVGQLERLsl 83
Cdd:cd07224   3 SFSAAGLLFPYHLGVLSLL-IEAGVINETTP-LAGASAGSLAAACSASGLSPEEAleaTEELAedcrsnGTAFRLGGV-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  84 silhpayapiehVKQQLQDALPPDAHVLASQ-RLGISLTR-WPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPP-E 160
Cdd:cd07224  79 ------------LRDELDKTLPDDAHERCNRgRIRVAVTQlFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLAPWPAtM 146

                       170       180       190
                ....*....|....*....|....*....|
gi 20304127 161 FRGERYIDGALSNNLP-FADCPSTITVSPF 189
Cdd:cd07224 147 FRGKLCVDGGFALFIPpTTAADRTVRVCPF 176
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 12-188 3.65e-19

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: 84.00  E-value: 3.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  12 LSFSGAGYLGAHHVGATECLRQRAPrlLQGARRIYGSSSGALNAVSIvcgksvdfccSHLLGMVGQLERlslsilhpaya 91
Cdd:cd01819   1 LSFSGGGFRGMYHAGVLSALAERGL--LDCVTYLAGTSGGAWVAATL----------YPPSSSLDNKPR----------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  92 piehvkQQLQDALppdahvlaSQRLGISLTRWPDGRNFLVTDFATCDELIQALVCTLYFPFYCGLIPP----------EF 161
Cdd:cd01819  58 ------QSLEEAL--------SGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKE 123

                       170       180       190
                ....*....|....*....|....*....|..
gi 20304127 162 RGERYIDGALSNNLPFADCPS-----TITVSP 188
Cdd:cd01819 124 KGVRLVDGGVSNNLPAPVLLRpgrgvTLTISP 155
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 12-177 4.33e-17

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: 79.19  E-value: 4.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127    12 LSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVD-------------FCCSHLLGMVGQL 78
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDPEeiedllleldlnlFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127    79 ERLSLSILHPAYAPIEHVKQQLQDALPPD-------------AHVLASQRLGISLTRWPDGRNFLVTDFATCDELIQALV 145
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLtleelaarlslllVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 20304127   146 CTLYFPFYcgLIPPEFRGERYIDGALSNNLPF 177
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 9-253 2.66e-11

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 63.77  E-value: 2.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127   9 RWNLSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVDFCCSHLLGM----------VGQL 78
Cdd:COG1752   6 KIGLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSADELEELWRSLdrrdlfdlslPRRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  79 ERLSLSILHPAYAPIEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVTDfatcDELIQALVCTLYFPfycGLIP 158
Cdd:COG1752  82 LRLDLGLSPGGLLDGDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDS----GPLADAVRASAAIP---GVFP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 159 P-EFRGERYIDGALSNNLPF-----ADCPSTITVSPFHgtvdicPQSTSPNLHEL--NVFNFSFQISTENFFLGLIC--L 228
Cdd:COG1752 155 PvEIDGRLYVDGGVVNNLPVdparaLGADRVIAVDLNP------PLRKLPSLLDIlgRALEIMFNSILRRELALEPAdiL 228

                       250       260       270
                ....*....|....*....|....*....|...
gi 20304127 229 IPPSL--------EVVADNCRQGYLDALRFLER 253
Cdd:COG1752 229 IEPDLsgislldfSRAEELIEAGYEAARRALDE 261
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 12-252 4.56e-08

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: 53.45  E-value: 4.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  12 LSFSGAGYLGAHHVGATECLRQRAPRLlqgaRRIYGSSSGALNAVSIVCGKSvdfccshllGMVGQLERLSLSIlhpAYA 91
Cdd:cd07209   1 LVLSGGGALGAYQAGVLKALAEAGIEP----DIISGTSIGAINGALIAGGDP---------EAVERLEKLWREL---SRE 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  92 PIeHVKQQLQDALPPDahvlasqRLGISLTRWPDGRNFLVTDFA---------TCDELIQALVCTLYFPfycGLIPP-EF 161
Cdd:cd07209  65 DV-FLRGLLDRALDFD-------TLRLLAILFAGLVIVAVNVLTgepvyfddiPDGILPEHLLASAALP---PFFPPvEI 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127 162 RGERYIDGALSNNLPfadcpstitVSPF--HG--TVDICPQSTSPNLHELNVFNFSFQISTENFFLGLicliPPSLEVVA 237
Cdd:cd07209 134 DGRYYWDGGVVDNTP---------LSPAidLGadEIIVVSLSDKGRDDRKGTPPTTLIEILPRLFLRS----GLDSERIR 200

                       250
                ....*....|....*
gi 20304127 238 DNCRQGYLDALRFLE 252
Cdd:cd07209 201 HNLELGYLDTLRADS 215
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 11-177 2.11e-05

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: 45.41  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  11 NLSFSGAGYLGAHHVGATECLRQRAPRLlqgaRRIYGSSSGALNAVSIVCGKSVDFCCSHLLGMvgqlERLSLSILHPAY 90
Cdd:cd07210   2 ALVLSSGFFGFYAHLGFLAALLEMGLEP----SAISGTSAGALVGGLFASGISPDEMAELLLSL----ERKDFWMFWDPP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304127  91 AP-----IEHVKQQLQDALPPDAHVLASQRLGISLTRWPDGRNFLVT--DFAtcdELIQAlVCTLYfPFYCgliPPEFRG 163
Cdd:cd07210  74 LRggllsGDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSegDLA---EAVAA-SCAVP-PLFQ---PVEIGG 145

                       170
                ....*....|....
gi 20304127 164 ERYIDGALSNNLPF 177
Cdd:cd07210 146 RPFVDGGVADRLPF 159
 
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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