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Conserved domains on  [gi|1820943769|ref|XP_032746790|]
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patatin-like phospholipase domain-containing protein 5 [Rattus rattus]

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), ...
 21-423 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: 850.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  21 MDFLEVEGGWSLSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVER 100
Cdd:cd07223     1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 101 LSLGIFHPAYGPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPA 180
Cdd:cd07223    81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 181 FRGERFIDGALSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYC 260
Cdd:cd07223   161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 261 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPALVEGPRGTDHSQGQEAGLIVRWDIPNVLVKDVPNFELLSPELEAALKK 340
Cdd:cd07223   241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 341 GCKRDFWAQIQ--CSVPGKVLTYLLLPCTLPFEYAYFRSRRLMQWLPDVPDDLYWMQGLLKSTTLEVYSMAKSWLLSLGS 418
Cdd:cd07223   321 ACTRDFSTWARfcCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                  ....*
gi 1820943769 419 PLVTS 423
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), ...
 21-423 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: 850.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  21 MDFLEVEGGWSLSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVER 100
Cdd:cd07223     1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 101 LSLGIFHPAYGPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPA 180
Cdd:cd07223    81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 181 FRGERFIDGALSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYC 260
Cdd:cd07223   161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 261 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPALVEGPRGTDHSQGQEAGLIVRWDIPNVLVKDVPNFELLSPELEAALKK 340
Cdd:cd07223   241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 341 GCKRDFWAQIQ--CSVPGKVLTYLLLPCTLPFEYAYFRSRRLMQWLPDVPDDLYWMQGLLKSTTLEVYSMAKSWLLSLGS 418
Cdd:cd07223   321 ACTRDFSTWARfcCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                  ....*
gi 1820943769 419 PLVTS 423
Cdd:cd07223   401 PPVTR 405
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 32-197 3.33e-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: 79.58  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQRAPRliqgARRFYGSSSGALNALSIICGKS-------------ADFACSNLLALVKHV 98
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDpeeiedllleldlNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  99 ERLSLGIFHPAYGPIEHIKKKLQDDLPDN-------------SHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALV 165
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLtleelaarlslllVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1820943769 166 CTLYFPFYcgTIPPAFRGERFIDGALSNNLPF 197
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 32-198 1.19e-10

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 61.84  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQR--APRLIqgarrfYGSSSGALNALSIICGKSAD--------FACSNLL--ALVKHVE 99
Cdd:COG1752     9 LVLSGGGARGAAHIGVLKALEEAgiPPDVI------AGTSAGAIVGALYAAGYSADeleelwrsLDRRDLFdlSLPRRLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 100 RLSLGIFHPAYGPIEHIKKKLQDDLPDNSHilasQRLGISLtrwpdgqnFIV-TDFAT-------RDELIQALVCTlyfp 171
Cdd:COG1752    83 RLDLGLSPGGLLDGDPLRRLLERLLGDRDF----EDLPIPL--------AVVaTDLETgrevvfdSGPLADAVRAS---- 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1820943769 172 fycGTIPPAFR-----GERFIDGALSNNLPFS 198
Cdd:COG1752   147 ---AAIPGVFPpveidGRLYVDGGVVNNLPVD 175
 
Name Accession Description Interval E-value
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 21-423 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: 850.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  21 MDFLEVEGGWSLSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVER 100
Cdd:cd07223     1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 101 LSLGIFHPAYGPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPA 180
Cdd:cd07223    81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 181 FRGERFIDGALSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYC 260
Cdd:cd07223   161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 261 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPALVEGPRGTDHSQGQEAGLIVRWDIPNVLVKDVPNFELLSPELEAALKK 340
Cdd:cd07223   241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 341 GCKRDFWAQIQ--CSVPGKVLTYLLLPCTLPFEYAYFRSRRLMQWLPDVPDDLYWMQGLLKSTTLEVYSMAKSWLLSLGS 418
Cdd:cd07223   321 ACTRDFSTWARfcCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                  ....*
gi 1820943769 419 PLVTS 423
Cdd:cd07223   401 PPVTR 405
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 31-273 6.05e-127

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: 367.83  E-value: 6.05e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  31 SLSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVERLSLGIFHPAY 110
Cdd:cd07204     1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 111 GPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPAFRGERFIDGA 190
Cdd:cd07204    81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 191 LSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYCRQGYLDALRF 270
Cdd:cd07204   161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                  ...
gi 1820943769 271 LER 273
Cdd:cd07204   241 LER 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 27-273 6.66e-103

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: 306.67  E-value: 6.66e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  27 EGGWSLSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVERLSLGIF 106
Cdd:cd07220     2 DSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 107 HPAYGPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPAFRGERF 186
Cdd:cd07220    82 HPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 187 IDGALSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYCRQGYLD 266
Cdd:cd07220   162 VDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRD 241


                  ....*..
gi 1820943769 267 ALRFLER 273
Cdd:cd07220   242 ALRFLKE 248
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 30-280 1.94e-94

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: 285.13  E-value: 1.94e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  30 WSLSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVERLSLGIFHPA 109
Cdd:cd07221     1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 110 YGPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPAFRGERFIDG 189
Cdd:cd07221    81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 190 ALSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYCRQGYLDALR 269
Cdd:cd07221   161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                         250
                  ....*....|.
gi 1820943769 270 FLERRGLTKEP 280
Cdd:cd07221   241 FLEENGICNRP 251
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 31-276 4.92e-90

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: 273.84  E-value: 4.92e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  31 SLSFSGSGYLGLYHVGVTECLRQRAPRLIQgaRRFYGSSSGALNALSIICGKSADFACSNLLALVKHVERLSLGIFHPAY 110
Cdd:cd07218     2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLL--NKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 111 GPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPAFRGERFIDGA 190
Cdd:cd07218    80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 191 LSNNLPfSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYCRQGYLDALRF 270
Cdd:cd07218   160 FSDNLP-TLDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRF 238


                  ....*.
gi 1820943769 271 LERRGL 276
Cdd:cd07218   239 LHRNNL 244
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 31-273 5.72e-68

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: 221.69  E-value: 5.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  31 SLSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVERLSLGIFHPAY 110
Cdd:cd07219    14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 111 GPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPAFRGERFIDGA 190
Cdd:cd07219    94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 191 LSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYCRQGYLDALRF 270
Cdd:cd07219   174 FTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLY 253


                  ...
gi 1820943769 271 LER 273
Cdd:cd07219   254 LRR 256
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 32-208 2.73e-58

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: 189.09  E-value: 2.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQRAPRliqgARRFYGSSSGALNALSIICGKSADFACSNLLALVKHVERLSLGIFHPAYG 111
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 112 PIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTdFATRDELIQALVCTLYFPFYCGTIPPAFRGERFIDGAL 191
Cdd:cd07198    77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                         170
                  ....*....|....*..
gi 1820943769 192 SNNLPFSYCPTTITVSP 208
Cdd:cd07198   156 SNNLPVAELGNTINVSP 172
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 32-275 1.62e-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: 189.85  E-value: 1.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQRAPRLIQGARRFYGSSSGALNA-LSIICGKSADFACSNLLALVKHVERLSLGIFHPAY 110
Cdd:cd07222     2 LSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAaVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 111 GPIEHIKKKLQDDLPDNSHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPAFRGERFIDGA 190
Cdd:cd07222    82 DFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 191 LSNNLPFSYCPTTITVSPFNGTVDICPQSTSSSLFELTAFNASFQISTRNFFLGFKSLFPPKPEVVADYCRQGYLDALRF 270
Cdd:cd07222   162 FTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVRF 241


                  ....*
gi 1820943769 271 LERRG 275
Cdd:cd07222   242 LKKEN 246
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 32-208 1.15e-20

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: 88.24  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQRAPRliQGARRFYGSSSGALNAlSIICGKSADFacsnllalvkhverlslgifhpayg 111
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERGLL--DCVTYLAGTSGGAWVA-ATLYPPSSSL------------------------- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 112 piehikkklqDDLPDNSHILASQ-RLGISLTRWPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPA---------- 180
Cdd:cd01819    53 ----------DNKPRQSLEEALSgKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPAelytsksnlk 122

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1820943769 181 FRGERFIDGALSNNLPFSYCP-----TTITVSP 208
Cdd:cd01819   123 EKGVRLVDGGVSNNLPAPVLLrpgrgVTLTISP 155
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 33-273 9.41e-20

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: 87.78  E-value: 9.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  33 SFSGSGYLGLYHVGVTECLRQRAprLIQGARRFYGSSSGALNALSIICGKSAD---FACSNLLALV-KHVERLSLGifhp 108
Cdd:cd07224     3 SFSAAGLLFPYHLGVLSLLIEAG--VINETTPLAGASAGSLAAACSASGLSPEealEATEELAEDCrSNGTAFRLG---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 109 aygpiEHIKKKLQDDLPDNSHILASQ-RLGISLTR-WPDGQNFIVTDFATRDELIQALVCTLYFPFYCGTIPPA-FRGER 185
Cdd:cd07224    77 -----GVLRDELDKTLPDDAHERCNRgRIRVAVTQlFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLAPWPATmFRGKL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 186 FIDGALSNNLPfsycPTTITvspfNGTVDICPqstssslFELTAFNASFQ-ISTRNFFLG--------FKSLFPPKPEVV 256
Cdd:cd07224   152 CVDGGFALFIP----PTTAA----DRTVRVCP-------FPASRSSIKGQnLDNDDTEDVpysrrqllNWALEPADDAML 216

                         250
                  ....*....|....*..
gi 1820943769 257 ADYCRQGYLDALRFLER 273
Cdd:cd07224   217 LELFNEGYKDANEWAKE 233
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 32-197 3.33e-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: 79.58  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQRAPRliqgARRFYGSSSGALNALSIICGKS-------------ADFACSNLLALVKHV 98
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDpeeiedllleldlNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  99 ERLSLGIFHPAYGPIEHIKKKLQDDLPDN-------------SHILASQRLGISLTRWPDGQNFIVTDFATRDELIQALV 165
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLtleelaarlslllVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1820943769 166 CTLYFPFYcgTIPPAFRGERFIDGALSNNLPF 197
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 32-198 1.19e-10

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 61.84  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQR--APRLIqgarrfYGSSSGALNALSIICGKSAD--------FACSNLL--ALVKHVE 99
Cdd:COG1752     9 LVLSGGGARGAAHIGVLKALEEAgiPPDVI------AGTSAGAIVGALYAAGYSADeleelwrsLDRRDLFdlSLPRRLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 100 RLSLGIFHPAYGPIEHIKKKLQDDLPDNSHilasQRLGISLtrwpdgqnFIV-TDFAT-------RDELIQALVCTlyfp 171
Cdd:COG1752    83 RLDLGLSPGGLLDGDPLRRLLERLLGDRDF----EDLPIPL--------AVVaTDLETgrevvfdSGPLADAVRAS---- 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1820943769 172 fycGTIPPAFR-----GERFIDGALSNNLPFS 198
Cdd:COG1752   147 ---AAIPGVFPpveidGRLYVDGGVVNNLPVD 175
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 32-198 4.64e-06

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: 47.29  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQRAPR--LIqgarrfYGSSSGALNALSIICGKSADfacsnllalVKHVERLSLGIfhpa 109
Cdd:cd07209     1 LVLSGGGALGAYQAGVLKALAEAGIEpdII------SGTSIGAINGALIAGGDPEA---------VERLEKLWREL---- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 110 ygpieHIKKKLQDDLPDnSHILASqRLGISLTRWPDGQNFIVTDFA---------TRDELIQALVCTlyfpfycGTIPPA 180
Cdd:cd07209    62 -----SREDVFLRGLLD-RALDFD-TLRLLAILFAGLVIVAVNVLTgepvyfddiPDGILPEHLLAS-------AALPPF 127

                         170       180
                  ....*....|....*....|...
gi 1820943769 181 FR-----GERFIDGALSNNLPFS 198
Cdd:cd07209   128 FPpveidGRYYWDGGVVDNTPLS 150
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 31-198 1.49e-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: 43.10  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  31 SLSFSGSGYLGLYHVGVTECLRQRAPRLiqgaRRFYGSSSGALNALSIICGKSadfaCSNLLALVKHVERLSLGIFH--P 108
Cdd:cd07210     2 ALVLSSGFFGFYAHLGFLAALLEMGLEP----SAISGTSAGALVGGLFASGIS----PDEMAELLLSLERKDFWMFWdpP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769 109 AYGPIEHIKK---KLQDDLPDNSHILASQRLGISLTRWPDGQNFIVT--DFAtrdELIQAlVCTLYfPFYCgtiPPAFRG 183
Cdd:cd07210    74 LRGGLLSGDRfaaLLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSegDLA---EAVAA-SCAVP-PLFQ---PVEIGG 145

                         170
                  ....*....|....*
gi 1820943769 184 ERFIDGALSNNLPFS 198
Cdd:cd07210   146 RPFVDGGVADRLPFD 160
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 32-80 1.62e-04

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: 43.35  E-value: 1.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLRQRA--PRLIQgarrfyGSSSGALNAlSIIC 80
Cdd:cd07206    72 LMLSGGASLGLFHLGVVKALWEQDllPRVIS------GSSAGAIVA-ALLG 115
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 32-196 3.20e-03

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: 38.80  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  32 LSFSGSGYLGLYHVGVTECLrQRAPRLIqgaRRFYGSSSGALNALSIICG-KSADFA------------------CSNLL 92
Cdd:cd07207     2 LVFEGGGAKGIAYIGALKAL-EEAGILK---KRVAGTSAGAITAALLALGySAADIKdilketdfaklldspvglLFLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820943769  93 ALVKhverlSLGIF--HPAYGPIEH-IKKKLQDDLPDNSHILASQRLGISL----TRWPDGQNFIVTDFATRDELI-QAL 164
Cdd:cd07207    78 SLFK-----EGGLYkgDALEEWLRElLKEKTGNSFATSLLRDLDDDLGKDLkvvaTDLTTGALVVFSAETTPDMPVaKAV 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1820943769 165 VCTLYFPFYcgtippaF------RGERFIDGALSNNLP 196
Cdd:cd07207   153 RASMSIPFV-------FkpvrlaKGDVYVDGGVLDNYP 183
 
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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