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Conserved domains on  [gi|123796300|sp|Q32LZ8|]
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RecName: Full=Patatin-like phospholipase domain-containing protein 5

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), ...
1-403 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: 850.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   1 MDFLEAEGGWNLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVER 80
Cdd:cd07223    1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  81 LSLGIFHPAYGPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPA 160
Cdd:cd07223   81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 161 FRGQRFIDGALSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHC 240
Cdd:cd07223  161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPALVEGPRGTGHDQGQKTGPTVRWDIPNVLVKDVPNFELLSPELEAALRK 320
Cdd:cd07223  241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 321 ACKRDFWTRVQ--CSVPGKVLAYLLLPCTLPFEYAYFRSRRLMEWLPEAPDDLDWMRSILKSTTLEVYSMAKSWLLRLGS 398
Cdd:cd07223  321 ACTRDFSTWARfcCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400

                 ....*
gi 123796300 399 PPGTR 403
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), ...
1-403 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: 850.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   1 MDFLEAEGGWNLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVER 80
Cdd:cd07223    1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  81 LSLGIFHPAYGPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPA 160
Cdd:cd07223   81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 161 FRGQRFIDGALSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHC 240
Cdd:cd07223  161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPALVEGPRGTGHDQGQKTGPTVRWDIPNVLVKDVPNFELLSPELEAALRK 320
Cdd:cd07223  241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 321 ACKRDFWTRVQ--CSVPGKVLAYLLLPCTLPFEYAYFRSRRLMEWLPEAPDDLDWMRSILKSTTLEVYSMAKSWLLRLGS 398
Cdd:cd07223  321 ACTRDFSTWARfcCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400

                 ....*
gi 123796300 399 PPGTR 403
Cdd:cd07223  401 PPVTR 405
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
12-177 1.21e-13

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: 69.18  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   12 LSFSGSGYMGLYHVGVTQCLRQRAPRliqgARRFYGSSSGALNAMAIVFGKS-------------ADFACSNLLDLVKLV 78
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDpeeiedllleldlNLFLSLIRKRALSLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   79 ERLSLGIFHPAYGPAEHIRKKLYENLPDN-------------CHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALI 145
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLtleelaarlslllVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 123796300  146 CTLYLPLYCGviPPAFRGQRFIDGALSNNLPF 177
Cdd:pfam01734 157 ASSALPGVFP--PVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
11-253 4.89e-13

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 68.78  E-value: 4.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLRQR--APRLIqgarrfYGSSSGALNAMAIVFGKSAD--------FACSNLLD--LVKLV 78
Cdd:COG1752    8 GLVLSGGGARGAAHIGVLKALEEAgiPPDVI------AGTSAGAIVGALYAAGYSADeleelwrsLDRRDLFDlsLPRRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  79 ERLSLGIFHPAYGPAEHIRKKLYENLPDN----CHIlasqRLGISMTRWPDGKNFIVTdfatRDEFIQALICTLYLPlyc 154
Cdd:COG1752   82 LRLDLGLSPGGLLDGDPLRRLLERLLGDRdfedLPI----PLAVVATDLETGREVVFD----SGPLADAVRASAAIP--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 155 GVIPP-AFRGQRFIDGALSNNLPFS----DCPTTITVSPFNGTVDICPqnishSLFELT--AFNASFQISTRNFFRGLKS 227
Cdd:COG1752  151 GVFPPvEIDGRLYVDGGVVNNLPVDparaLGADRVIAVDLNPPLRKLP-----SLLDILgrALEIMFNSILRRELALEPA 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 123796300 228 VFPPKPEV----------VADHCRQGYLDALRFLER 253
Cdd:COG1752  226 DILIEPDLsgislldfsrAEELIEAGYEAARRALDE 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), ...
1-403 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: 850.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   1 MDFLEAEGGWNLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVER 80
Cdd:cd07223    1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  81 LSLGIFHPAYGPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPA 160
Cdd:cd07223   81 LSLGIFHPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 161 FRGQRFIDGALSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHC 240
Cdd:cd07223  161 FRGERYIDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPALVEGPRGTGHDQGQKTGPTVRWDIPNVLVKDVPNFELLSPELEAALRK 320
Cdd:cd07223  241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 321 ACKRDFWTRVQ--CSVPGKVLAYLLLPCTLPFEYAYFRSRRLMEWLPEAPDDLDWMRSILKSTTLEVYSMAKSWLLRLGS 398
Cdd:cd07223  321 ACTRDFSTWARfcCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400

                 ....*
gi 123796300 399 PPGTR 403
Cdd:cd07223  401 PPVTR 405
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
11-253 7.01e-120

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: 348.96  E-value: 7.01e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVERLSLGIFHPAY 90
Cdd:cd07204    1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  91 GPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPAFRGQRFIDGA 170
Cdd:cd07204   81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 171 LSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHCRQGYLDALRF 250
Cdd:cd07204  161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240

                 ...
gi 123796300 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 4.43e-107

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: 316.69  E-value: 4.43e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   7 EGGWNLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVERLSLGIF 86
Cdd:cd07220    2 DSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  87 HPAYGPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPAFRGQRF 166
Cdd:cd07220   82 HPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 167 IDGALSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHCRQGYLD 246
Cdd:cd07220  162 VDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRD 241

                 ....*..
gi 123796300 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 3.56e-91

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: 276.27  E-value: 3.56e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  10 WNLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVERLSLGIFHPA 89
Cdd:cd07221    1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  90 YGPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPAFRGQRFIDG 169
Cdd:cd07221   81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 170 ALSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHCRQGYLDALR 249
Cdd:cd07221  161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240
                        250
                 ....*....|.
gi 123796300 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 2.68e-88

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: 268.44  E-value: 2.68e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLRQRAPRLIQgaRRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVERLSLGIFHPAY 90
Cdd:cd07218    2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLL--NKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  91 GPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPAFRGQRFIDGA 170
Cdd:cd07218   80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 171 LSNNLPFSDcPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHCRQGYLDALRF 250
Cdd:cd07218  160 FSDNLPTLD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRF 238

                 ....*.
gi 123796300 251 LERRGL 256
Cdd:cd07218  239 LHRNNL 244
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
11-253 6.88e-63

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: 207.82  E-value: 6.88e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVERLSLGIFHPAY 90
Cdd:cd07219   14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  91 GPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPAFRGQRFIDGA 170
Cdd:cd07219   94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 171 LSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHCRQGYLDALRF 250
Cdd:cd07219  174 FTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLY 253

                 ...
gi 123796300 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 1.38e-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: 189.46  E-value: 1.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLRQRAPRLIQGARRFYGSSSGALNAMAIVFG-KSADFACSNLLDLVKLVERLSLGIFHPA 89
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTApEKIEECKEFTYKFAEEVRKQRFGAMTPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  90 YGPAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPAFRGQRFIDG 169
Cdd:cd07222   81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 170 ALSNNLPFSDCPTTITVSPFNGTVDICPQNISHSLFELTAFNASFQISTRNFFRGLKSVFPPKPEVVADHCRQGYLDALR 249
Cdd:cd07222  161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240

                 ....*.
gi 123796300 250 FLERRG 255
Cdd:cd07222  241 FLKKEN 246
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
12-188 2.53e-55

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 181.00  E-value: 2.53e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  12 LSFSGSGYMGLYHVGVTQCLRQRAPRliqgARRFYGSSSGALNAMAIVFGKSADFACSNLLDLVKLVERLSLGIFHPAYG 91
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  92 PAEHIRKKLYENLPDNCHILASQRLGISMTRWPDGKNFIVTdFATRDEFIQALICTLYLPLYCGVIPPAFRGQRFIDGAL 171
Cdd:cd07198   77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155
                        170
                 ....*....|....*..
gi 123796300 172 SNNLPFSDCPTTITVSP 188
Cdd:cd07198  156 SNNLPVAELGNTINVSP 172
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
13-210 4.51e-21

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: 91.25  E-value: 4.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  13 SFSGSGYMGLYHVGVTQCLRQRAprLIQGARRFYGSSSGALNAMAIVFGKSAD---FACSNLL-DLVKLVERLSLGifhp 88
Cdd:cd07224    3 SFSAAGLLFPYHLGVLSLLIEAG--VINETTPLAGASAGSLAAACSASGLSPEealEATEELAeDCRSNGTAFRLG---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  89 aygpaEHIRKKLYENLPDNCHILASQ-RLGISMTR-WPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPA-FRGQR 165
Cdd:cd07224   77 -----GVLRDELDKTLPDDAHERCNRgRIRVAVTQlFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLAPWPATmFRGKL 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 123796300 166 FIDGALSNNLP-FSDCPTTITVSPFN-GTVDICPQNISHSLFELTAF 210
Cdd:cd07224  152 CVDGGFALFIPpTTAADRTVRVCPFPaSRSSIKGQNLDNDDTEDVPY 198
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
12-188 1.43e-18

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: 82.08  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  12 LSFSGSGYMGLYHVGVTQCLRQRAPRliQGARRFYGSSSGALnAMAIVFGKSADFacsnlldLVKLVERLSLgifhpayg 91
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLL--DCVTYLAGTSGGAW-VAATLYPPSSSL-------DNKPRQSLEE-------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  92 paehirkklyenlpdnchiLASQRLGISMTRWPDGKNFIVTDFATRDEFIQALICTLYLPLYCGVIPPA----------F 161
Cdd:cd01819   63 -------------------ALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPAelytsksnlkE 123
                        170       180       190
                 ....*....|....*....|....*....|..
gi 123796300 162 RGQRFIDGALSNNLPFSDCP-----TTITVSP 188
Cdd:cd01819  124 KGVRLVDGGVSNNLPAPVLLrpgrgVTLTISP 155
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
12-177 1.21e-13

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: 69.18  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   12 LSFSGSGYMGLYHVGVTQCLRQRAPRliqgARRFYGSSSGALNAMAIVFGKS-------------ADFACSNLLDLVKLV 78
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDpeeiedllleldlNLFLSLIRKRALSLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300   79 ERLSLGIFHPAYGPAEHIRKKLYENLPDN-------------CHILASQRLGISMTRWPDGKNFIVTDFATRDEFIQALI 145
Cdd:pfam01734  77 ALLRGLIGEGGLFDGDALRELLRKLLGDLtleelaarlslllVVALRALLTVISTALGTRARILLPDDLDDDEDLADAVL 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 123796300  146 CTLYLPLYCGviPPAFRGQRFIDGALSNNLPF 177
Cdd:pfam01734 157 ASSALPGVFP--PVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
11-253 4.89e-13

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 68.78  E-value: 4.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLRQR--APRLIqgarrfYGSSSGALNAMAIVFGKSAD--------FACSNLLD--LVKLV 78
Cdd:COG1752    8 GLVLSGGGARGAAHIGVLKALEEAgiPPDVI------AGTSAGAIVGALYAAGYSADeleelwrsLDRRDLFDlsLPRRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  79 ERLSLGIFHPAYGPAEHIRKKLYENLPDN----CHIlasqRLGISMTRWPDGKNFIVTdfatRDEFIQALICTLYLPlyc 154
Cdd:COG1752   82 LRLDLGLSPGGLLDGDPLRRLLERLLGDRdfedLPI----PLAVVATDLETGREVVFD----SGPLADAVRASAAIP--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300 155 GVIPP-AFRGQRFIDGALSNNLPFS----DCPTTITVSPFNGTVDICPqnishSLFELT--AFNASFQISTRNFFRGLKS 227
Cdd:COG1752  151 GVFPPvEIDGRLYVDGGVVNNLPVDparaLGADRVIAVDLNPPLRKLP-----SLLDILgrALEIMFNSILRRELALEPA 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 123796300 228 VFPPKPEV----------VADHCRQGYLDALRFLER 253
Cdd:COG1752  226 DILIEPDLsgislldfsrAEELIEAGYEAARRALDE 261
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
12-65 1.77e-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: 1.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 123796300  12 LSFSGSGYMGLYHVGVTQCLRQRA--PRLIQgarrfyGSSSGALnaMAIVFGKSAD 65
Cdd:cd07206   72 LMLSGGASLGLFHLGVVKALWEQDllPRVIS------GSSAGAI--VAALLGTHTD 119
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
12-178 1.92e-04

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: 42.66  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  12 LSFSGSGYMGLYHVGVTQCLRQRAPR--LIqgarrfYGSSSGALNAMAIvfgksadfaCSNLLDLVKLVERLSLGIfhpa 89
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEpdII------SGTSIGAINGALI---------AGGDPEAVERLEKLWREL---- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  90 ygpaeHIRKKLYENLPDNcHILASqRLGISMTRWPDGKNFIVTDFATRDEFI---------QALICTlylplycGVIPPA 160
Cdd:cd07209   62 -----SREDVFLRGLLDR-ALDFD-TLRLLAILFAGLVIVAVNVLTGEPVYFddipdgilpEHLLAS-------AALPPF 127
                        170       180
                 ....*....|....*....|...
gi 123796300 161 FR-----GQRFIDGALSNNLPFS 178
Cdd:cd07209  128 FPpveidGRYYWDGGVVDNTPLS 150
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
11-176 1.12e-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: 39.96  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLrQRAPRLIqgaRRFYGSSSGALNAMAIVFGKSADfacsnllDLVKLVERLSLGIFHPAY 90
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKAL-EEAGILK---KRVAGTSAGAITAALLALGYSAA-------DIKDILKETDFAKLLDSP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  91 GPAEH----------------IRKKLYENLPDNCHILASQRLGISMTrwPDGK---NFIVTDFATRDEFIQALICTLYLP 151
Cdd:cd07207   70 VGLLFllpslfkegglykgdaLEEWLRELLKEKTGNSFATSLLRDLD--DDLGkdlKVVATDLTTGALVVFSAETTPDMP 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 123796300 152 LYCGV-----IPPAF------RGQRFIDGALSNNLP 176
Cdd:cd07207  148 VAKAVrasmsIPFVFkpvrlaKGDVYVDGGVLDNYP 183
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
11-178 7.15e-03

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: 37.71  E-value: 7.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  11 NLSFSGSGYMGLYHVGVTQCLRQRAPRLiqgaRRFYGSSSGALNAMAIVFGKSadfaCSNLLDLVKLVERLSLGIFH--P 88
Cdd:cd07210    2 ALVLSSGFFGFYAHLGFLAALLEMGLEP----SAISGTSAGALVGGLFASGIS----PDEMAELLLSLERKDFWMFWdpP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796300  89 AYGPAEHIRK---KLYENLPdnchilaSQRlgISMTRWPdgKNFIVTDFATRDEF-------IQALI--CTLYlPLYCgv 156
Cdd:cd07210   74 LRGGLLSGDRfaaLLREHLP-------PDR--FEELRIP--LAVSVVDLTSRETLllsegdlAEAVAasCAVP-PLFQ-- 139
                        170       180
                 ....*....|....*....|..
gi 123796300 157 iPPAFRGQRFIDGALSNNLPFS 178
Cdd:cd07210  140 -PVEIGGRPFVDGGVADRLPFD 160
 
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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