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Conserved domains on  [gi|56757334|gb|AAW26838|]
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SJCHGC06417 protein [Schistosoma japonicum]

Protein Classification

patatin-like phospholipase domain-containing protein( domain architecture ID 27818)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Patatin_and_cPLA2 super family cl11396
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 23-282 7.16e-143

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


The actual alignment was detected with superfamily member cd07218:

Pssm-ID: 416256  Cd Length: 245  Bit Score: 406.35  E-value: 7.16e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  23 HNLSFAGCGFLGLYHIGVCSCIKRFAPHLYQNKpVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRF 102
Cdd:cd07218   1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK-ISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 KISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGG 182
Cdd:cd07218  80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 183 LSDNLLNINQQTIKVSPFAGDSDICPLESKWGPQyhrdqpqkyedvlgSISLLNLTMSFNLTNIKRLVGMVWPMTPDQLV 262
Cdd:cd07218 160 FSDNLPTLDENTITVSPFCGESDICPRDNSSQLF--------------HINWANTSIELSRQNIYRLVRILFPPRPEVLS 225

                       250       260
                ....*....|....*....|
gi 56757334 263 NLTNQGYDDALRFLITRGFI 282
Cdd:cd07218 226 SLCQQGFDDALRFLHRNNLI 245
 
Name Accession Description Interval E-value
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 23-282 7.16e-143

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: 406.35  E-value: 7.16e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  23 HNLSFAGCGFLGLYHIGVCSCIKRFAPHLYQNKpVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRF 102
Cdd:cd07218   1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK-ISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 KISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGG 182
Cdd:cd07218  80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 183 LSDNLLNINQQTIKVSPFAGDSDICPLESKWGPQyhrdqpqkyedvlgSISLLNLTMSFNLTNIKRLVGMVWPMTPDQLV 262
Cdd:cd07218 160 FSDNLPTLDENTITVSPFCGESDICPRDNSSQLF--------------HINWANTSIELSRQNIYRLVRILFPPRPEVLS 225

                       250       260
                ....*....|....*....|
gi 56757334 263 NLTNQGYDDALRFLITRGFI 282
Cdd:cd07218 226 SLCQQGFDDALRFLHRNNLI 245
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 25-187 2.36e-20

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: 88.05  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334    25 LSFAGCGFLGLYHIGVcscIKRFAPHLYQNKPVSGTSAGALAAACLVCDLDIDECVRYLCRIIENA-------------- 90
Cdd:pfam01734   1 LVLSGGGARGAYHLGV---LKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralslla 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334    91 ---RQFTLGPFDPRFKISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKY---------KSKDELIQALLC 158
Cdd:pfam01734  78 llrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRarillpddlDDDEDLADAVLA 157

                         170       180
                  ....*....|....*....|....*....
gi 56757334   159 SAYIPVFsgFVPLTFRGQLVIDGGLSDNL 187
Cdd:pfam01734 158 SSALPGV--FPPVRLDGELYVDGGLVDNV 184
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 22-187 1.37e-17

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 81.87  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  22 KHNLSFAGCGFLGLYHIGVcscIKRFAPHlyQNKP--VSGTSAGALAAACLVCDLDIDECVRYLCRI-IENARQFTLGPF 98
Cdd:COG1752   6 KIGLVLSGGGARGAAHIGV---LKALEEA--GIPPdvIAGTSAGAIVGALYAAGYSADELEELWRSLdRRDLFDLSLPRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  99 DPRFKISeYLKDGLI------QLLpqDAHVICSD--RLSISLTCFAT----GKNIVVRkyksKDELIQALLCSAYIPVFs 166
Cdd:COG1752  81 LLRLDLG-LSPGGLLdgdplrRLL--ERLLGDRDfeDLPIPLAVVATdletGREVVFD----SGPLADAVRASAAIPGV- 152

                       170       180
                ....*....|....*....|.
gi 56757334 167 gFVPLTFRGQLVIDGGLSDNL 187
Cdd:COG1752 153 -FPPVEIDGRLYVDGGVVNNL 172
 
Name Accession Description Interval E-value
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 23-282 7.16e-143

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: 406.35  E-value: 7.16e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  23 HNLSFAGCGFLGLYHIGVCSCIKRFAPHLYQNKpVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRF 102
Cdd:cd07218   1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK-ISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 KISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGG 182
Cdd:cd07218  80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 183 LSDNLLNINQQTIKVSPFAGDSDICPLESKWGPQyhrdqpqkyedvlgSISLLNLTMSFNLTNIKRLVGMVWPMTPDQLV 262
Cdd:cd07218 160 FSDNLPTLDENTITVSPFCGESDICPRDNSSQLF--------------HINWANTSIELSRQNIYRLVRILFPPRPEVLS 225

                       250       260
                ....*....|....*....|
gi 56757334 263 NLTNQGYDDALRFLITRGFI 282
Cdd:cd07218 226 SLCQQGFDDALRFLHRNNLI 245
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 24-276 7.02e-89

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: 268.84  E-value: 7.02e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  24 NLSFAGCGFLGLYHIGVCSCIKRFAPHLYQN-KPVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRF 102
Cdd:cd07204   1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNaRRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 KISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGG 182
Cdd:cd07204  81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 183 LSDNL-LNINQQTIKVSPFAGDSDICPLEskWGPQYHRdqpqkyedvlgsISLLNLTMSFNLTNIKRLVGMVWPMTPDQL 261
Cdd:cd07204 161 LSDNLpILDDENTITVSPFSGESDICPQD--KSSNLLE------------VNIANTSIQLSLENLYRLNRALFPPSLEIL 226

                       250
                ....*....|....*
gi 56757334 262 VNLTNQGYDDALRFL 276
Cdd:cd07204 227 SRMCQQGYLDALRFL 241
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 24-276 5.73e-78

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: 241.19  E-value: 5.73e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  24 NLSFAGCGFLGLYHIGVCSCIKRFAPHLYQN-KPVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRF 102
Cdd:cd07220   6 NISFAGCGFLGVYHVGVASCLLEHAPFLVANaRKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPLHPSF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 KISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGG 182
Cdd:cd07220  86 NLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRYVDGG 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 183 LSDNL-LNINQQTIKVSPFAGDSDICPleskwgpqyhRDqpqkyedvlGSISLLNLTMS-----FNLTNIKRLVGMVWPM 256
Cdd:cd07220 166 ISDNLpQYELKNTITVSPFSGESDICP----------RD---------SSTNFHELRFTntsiqFNLRNLYRLSKALFPP 226

                       250       260
                ....*....|....*....|
gi 56757334 257 TPDQLVNLTNQGYDDALRFL 276
Cdd:cd07220 227 EPQVLAEMCKQGYRDALRFL 246
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 24-276 5.56e-64

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: 205.26  E-value: 5.56e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  24 NLSFAGCGFLGLYHIGVCSCIKRFAPHLYQN-KPVSGTSAGALAAACLVCDLD-IDECVRYLCRIIENARQFTLGPFDPR 101
Cdd:cd07222   1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRvKRFAGASAGSLVAAVLLTAPEkIEECKEFTYKFAEEVRKQRFGAMTPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 102 FKISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDG 181
Cdd:cd07222  81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 182 GLSDNL-LNINQQTIKVSPFAGDSDICPLeskwgpqyHRDQPQKYedvlgsISLLNLTMSFNLTNIKRLVGMVWPMTPDQ 260
Cdd:cd07222 161 GFTNSLpVLPVGRTITVSPFSGRADICPQ--------DKGQLDLY------VRFANQDIMLSLANLVRLNQALFPPNRRK 226

                       250
                ....*....|....*.
gi 56757334 261 LVNLTNQGYDDALRFL 276
Cdd:cd07222 227 LESYYQMGFDDAVRFL 242
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 24-280 1.18e-59

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: 194.22  E-value: 1.18e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  24 NLSFAGCGFLGLYHIGVCSCIKRFAPHLYQNKP-VSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRF 102
Cdd:cd07221   2 SLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARmFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 KISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGG 182
Cdd:cd07221  82 NLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDGG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 183 LSDNLLNIN-QQTIKVSPFAGDSDICPlESKWGPQYHRDqpqkyedvlgsisLLNLTMSFNLTNIKRLVGMVWPMTPDQL 261
Cdd:cd07221 162 VSDNVPFFDaKTTITVSPFYGEYDICP-KVKSTNFLHVD-------------FTKLSLRLCTENLYLLTRALFPPDVKVL 227

                       250
                ....*....|....*....
gi 56757334 262 VNLTNQGYDDALRFLITRG 280
Cdd:cd07221 228 GEICLRGYLDAFRFLEENG 246
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 24-281 1.34e-58

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: 196.29  E-value: 1.34e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  24 NLSFAGCGFLGLYHIGVCSCIKRFAPHLYQN-KPVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRF 102
Cdd:cd07223  11 NLSFSGAGYLGLYHVGVTECLRQRAPRLLQGaRRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIFHPAY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 KISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGG 182
Cdd:cd07223  91 APIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDGA 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 183 LSDNL-LNINQQTIKVSPFAGDSDICpleskwgpqyhrdqPQKYEDVLGSISLLNLTMSFNLTNIKRLVGMVWPMTPDQL 261
Cdd:cd07223 171 LSNNLpFSDCPSTITVSPFHGTVDIC--------------PQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVV 236

                       250       260
                ....*....|....*....|
gi 56757334 262 VNLTNQGYDDALRFLITRGF 281
Cdd:cd07223 237 ADNCRQGYLDALRFLERRGL 256
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 23-276 2.42e-55

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: 187.02  E-value: 2.42e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  23 HNLSFAGCGFLGLYHIGVCSCIKRFAPHLYQNK-PVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPR 101
Cdd:cd07219  13 HSISFSGSGFLSFYQAGVVDALRDLAPRMLETAhRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPS 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 102 FKISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDG 181
Cdd:cd07219  93 CKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDG 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 182 GLSD-NLLNINQQTIKVSPFAGDSDICPleskwgpqyhRDQPQKYEDvlgsISLLNLTMSFNLTNIKRLVGMVWPmtPDQ 260
Cdd:cd07219 173 GFTGmQPCSFWTDSITISTFSGQQDICP----------RDCPAIFHD----FRIFNCSFQFSLENIARMTHALFP--PDL 236

                       250
                ....*....|....*...
gi 56757334 261 LV--NLTNQGYDDALRFL 276
Cdd:cd07219 237 MVlhDYYYRGYQDTVLYL 254
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 25-187 1.22e-44

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: 152.50  E-value: 1.22e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  25 LSFAGCGFLGLYHIGVCSCIKRFAPHLyqnKPVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLGPFDPRFKI 104
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRERGPLI---DIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 105 SEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVrKYKSKDELIQALLCSAYIPVFSGFVPLTFRGQLVIDGGLS 184
Cdd:cd07198  78 LGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLV-SDTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGLS 156


                ...
gi 56757334 185 DNL 187
Cdd:cd07198 157 NNL 159
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 26-200 8.51e-30

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: 115.13  E-value: 8.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  26 SFAGCGFLGLYHIGVCSCIKRfAPHLYQNKPVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFTLgpfdpRFKIS 105
Cdd:cd07224   3 SFSAAGLLFPYHLGVLSLLIE-AGVINETTPLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNGT-----AFRLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 106 EYLKDGLIQLLPQDAHVICSD-RLSISLT-CFATGKNIVVRKYKSKDELIQALLCSAYIPV-FSGFVPLTFRGQLVIDGG 182
Cdd:cd07224  77 GVLRDELDKTLPDDAHERCNRgRIRVAVTqLFPVPRGLLVSSFDSKSDLIDALLASCNIPGyLAPWPATMFRGKLCVDGG 156

                       170       180
                ....*....|....*....|.
gi 56757334 183 LSDN---LLNINqQTIKVSPF 200
Cdd:cd07224 157 FALFippTTAAD-RTVRVCPF 176
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 25-187 2.36e-20

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: 88.05  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334    25 LSFAGCGFLGLYHIGVcscIKRFAPHLYQNKPVSGTSAGALAAACLVCDLDIDECVRYLCRIIENA-------------- 90
Cdd:pfam01734   1 LVLSGGGARGAYHLGV---LKALGEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralslla 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334    91 ---RQFTLGPFDPRFKISEYLKDGLIQLLPQDAHVICSDRLSISLTCFATGKNIVVRKY---------KSKDELIQALLC 158
Cdd:pfam01734  78 llrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRarillpddlDDDEDLADAVLA 157

                         170       180
                  ....*....|....*....|....*....
gi 56757334   159 SAYIPVFsgFVPLTFRGQLVIDGGLSDNL 187
Cdd:pfam01734 158 SSALPGV--FPPVRLDGELYVDGGLVDNV 184
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 25-187 1.56e-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: 84.77  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  25 LSFAGCGFLGLYHIGVCSCIKRFAPHLYQNKpVSGTSAGALAAACLVcdldidecvrylcriienarqftlgpfDPRFKI 104
Cdd:cd01819   1 LSFSGGGFRGMYHAGVLSALAERGLLDCVTY-LAGTSGGAWVAATLY---------------------------PPSSSL 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 105 SEYLKDGLIQLLpqdahvicSDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVPL----------TFR 174
Cdd:cd01819  53 DNKPRQSLEEAL--------SGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKEK 124

                       170
                ....*....|...
gi 56757334 175 GQLVIDGGLSDNL 187
Cdd:cd01819 125 GVRLVDGGVSNNL 137
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 22-187 1.37e-17

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 81.87  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  22 KHNLSFAGCGFLGLYHIGVcscIKRFAPHlyQNKP--VSGTSAGALAAACLVCDLDIDECVRYLCRI-IENARQFTLGPF 98
Cdd:COG1752   6 KIGLVLSGGGARGAAHIGV---LKALEEA--GIPPdvIAGTSAGAIVGALYAAGYSADELEELWRSLdRRDLFDLSLPRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  99 DPRFKISeYLKDGLI------QLLpqDAHVICSD--RLSISLTCFAT----GKNIVVRkyksKDELIQALLCSAYIPVFs 166
Cdd:COG1752  81 LLRLDLG-LSPGGLLdgdplrRLL--ERLLGDRDfeDLPIPLAVVATdletGREVVFD----SGPLADAVRASAAIPGV- 152

                       170       180
                ....*....|....*....|.
gi 56757334 167 gFVPLTFRGQLVIDGGLSDNL 187
Cdd:COG1752 153 -FPPVEIDGRLYVDGGVVNNL 172
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 25-187 2.25e-12

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 64.87  E-value: 2.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  25 LSFAGCGFLGLYHIGVcscIKRFA-----PHLyqnkpVSGTSAGALAAACLVCDLDIDECVRYLCRIIENARQFtlgpFD 99
Cdd:cd07205   3 LALSGGGARGLAHIGV---LKALEeagipIDI-----VSGTSAGAIVGALYAAGYSPEEIEERAKLRSTDLKAL----SD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 100 PRFKISEYLK-DGLIQLLPQDAHVICSDRLSISLTCFAT----GKNIVVRKykskDELIQALLCSAYIPVfsGFVPLTFR 174
Cdd:cd07205  71 LTIPTAGLLRgDKFLELLDEYFGDRDIEDLWIPFFIVATdltsGKLVVFRS----GSLVRAVRASMSIPG--IFPPVKID 144

                       170
                ....*....|...
gi 56757334 175 GQLVIDGGLSDNL 187
Cdd:cd07205 145 GQLLVDGGVLNNL 157
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 25-187 6.03e-12

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: 64.62  E-value: 6.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  25 LSFAGCGFLGLYHIGVcscIKRFAPHLYQNKPVSGTSAGALAAACLVCDLD--IDECVR----------YLCRIIENArq 92
Cdd:cd07209   1 LVLSGGGALGAYQAGV---LKALAEAGIEPDIISGTSIGAINGALIAGGDPeaVERLEKlwrelsredvFLRGLLDRA-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  93 ftlgpfdPRFKISEYLKDGLIqllpqdahvicsdRLSISLTCFATGKNIVVRKyKSKDELIQALLCSAYIPVFsgFVPLT 172
Cdd:cd07209  76 -------LDFDTLRLLAILFA-------------GLVIVAVNVLTGEPVYFDD-IPDGILPEHLLASAALPPF--FPPVE 132

                       170
                ....*....|....*
gi 56757334 173 FRGQLVIDGGLSDNL 187
Cdd:cd07209 133 IDGRYYWDGGVVDNT 147
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 25-187 6.27e-10

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 59.55  E-value: 6.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  25 LSFAGCGFLGLYHIGVCSCIKRfapHLYQNKP-VSGTSAGALAAAClvcdldidecvrYLCRIIENARQFTLGP-FDPRF 102
Cdd:cd07208   1 LVLEGGGMRGAYTAGVLDAFLE---AGIRPFDlVIGVSAGALNAAS------------YLSGQRGRALRINTKYaTDPRY 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 -KISEYLKDG------------LIQLLPQDAHVIC--SDRLSISLTCFATGKNIVVRKYKSKDELIQALLCSAYIPVFsg 167
Cdd:cd07208  66 lGLRSLLRTGnlfdldflydelPDGLDPFDFEAFAasPARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGL-- 143

                       170       180
                ....*....|....*....|
gi 56757334 168 FVPLTFRGQLVIDGGLSDNL 187
Cdd:cd07208 144 FPPVRIDGEPYVDGGLSDSI 163
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 24-187 1.03e-07

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: 51.90  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  24 NLSFAGCGFLGLYHIGVCSCIKRfapHLYQNKPVSGTSAGALAAACLVCDLDIDEcVRYLCRIIeNARQFTLGPFDPRFK 103
Cdd:cd07207   1 NLVFEGGGAKGIAYIGALKALEE---AGILKKRVAGTSAGAITAALLALGYSAAD-IKDILKET-DFAKLLDSPVGLLFL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 104 ISEYLKDG-----------------------LIQLLPQDAHVICSDRLSISLTCFATGKNIVvrkYKSKD----ELIQAL 156
Cdd:cd07207  76 LPSLFKEGglykgdaleewlrellkektgnsFATSLLRDLDDDLGKDLKVVATDLTTGALVV---FSAETtpdmPVAKAV 152

                       170       180       190
                ....*....|....*....|....*....|..
gi 56757334 157 LCSAYIPVFsgFVPLTF-RGQLVIDGGLSDNL 187
Cdd:cd07207 153 RASMSIPFV--FKPVRLaKGDVYVDGGVLDNY 182
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 31-187 4.00e-07

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: 50.42  E-value: 4.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  31 GFLGLY-HIGVCS-CIKR-FAPhlyqnKPVSGTSAGALAAACLVCDLDIDECVRYLCRIieNARQFTLGPFDPRF----- 102
Cdd:cd07210   8 GFFGFYaHLGFLAaLLEMgLEP-----SAISGTSAGALVGGLFASGISPDEMAELLLSL--ERKDFWMFWDPPLRgglls 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 103 --KISEYL-KDGLIQLLPQdahviCSDRLSISLTCFATGKnivvRKYKSKDELIQALLCSAYIPVFsgFVPLTFRGQLVI 179
Cdd:cd07210  81 gdRFAALLrEHLPPDRFEE-----LRIPLAVSVVDLTSRE----TLLLSEGDLAEAVAASCAVPPL--FQPVEIGGRPFV 149


                ....*...
gi 56757334 180 DGGLSDNL 187
Cdd:cd07210 150 DGGVADRL 157
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 34-187 1.31e-06

Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like phospholipase domain containing protein 6. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This group includes YCHK and rssA from Escherichia coli as well as Ylbk from Bacillus amyloliquefaciens.


Pssm-ID: 132866 [Multi-domain]  Cd Length: 175  Bit Score: 48.04  E-value: 1.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  34 GLYHIGVcscIKRFAPHLYQNKPVSGTSAGALAAACLVCDLDIDEcvryLCRIIENARQFTLGPFDPRFKISEYLK---- 109
Cdd:cd07228  12 GWAHIGV---LRALEEEGIEIDIIAGSSIGALVGALYAAGHLDAL----EEWVRSLSQRDVLRLLDLSASRSGLLKgekv 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 110 DGLIQLLPQDAHVicsDRLSISLTCFA----TGKNIVVRKYKskdeLIQALLCSAYIPVFsgFVPLTFRGQLVIDGGLSD 185
Cdd:cd07228  85 LEYLREIMGGVTI---EELPIPFAAVAtdlqTGKEVWFREGS----LIDAIRASISIPGI--FAPVEHNGRLLVDGGVVN 155


                ..
gi 56757334 186 NL 187
Cdd:cd07228 156 PI 157
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
57-185 8.35e-06

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 47.08  E-value: 8.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  57 VSGTSAGALAAAClvcdldidecvrYLCRIIENARQFTLGP-FDPRF-KISEYLKDG-------LIQLLPQ--------- 118
Cdd:COG4667  37 VIGVSAGALNGAS------------YLSRQPGRARRVITDYaTDPRFfSLRNFLRGGnlfdldfLYDEIPNellpfdfet 104

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56757334 119 ------DAHVICSDRlsisltcfATGKNIVVRKYKSKDELIQALLCSAYIPVFSGFVplTFRGQLVIDGGLSD 185
Cdd:COG4667 105 fkasprEFYVVATNA--------DTGEAEYFSKKDDDYDLLDALRASSALPLLYPPV--EIDGKRYLDGGVAD 167
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 25-268 2.52e-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: 42.58  E-value: 2.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334  25 LSFAGCGFLGLYHIGVCSCikrfaphLYQNK--P--VSGTSAGALAAACLVCDLDIDecvrylcriienarqfTLGpfDP 100
Cdd:cd07206  72 LMLSGGASLGLFHLGVVKA-------LWEQDllPrvISGSSAGAIVAALLGTHTDEE----------------LIG--DL 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 101 RFKiSEYLKDGL---IQLLPQDAHVicSDRlsisLTCFATGKNIVVRkykskdeliQALLCSAYIPVFSGFVPLTFR--- 174
Cdd:cd07206 127 TFQ-EAYERTGRiinITVAPAEPHQ--NSR----LLNALTSPNVLIW---------SAVLASCAVPGVFPPVMLMAKnrd 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56757334 175 GQLV--------IDGGLSDN--------LLNIN-----QQTIKVSPFAgdsdicpleskwgpqyhrdqpQKYEdvlGSIs 233
Cdd:cd07206 191 GEIVpylpgrkwVDGSVSDDlpakrlarLYNVNhfivsQTNPHVVPFL---------------------QEYS---GDI- 245

                       250       260       270
                ....*....|....*....|....*....|....*
gi 56757334 234 llNLTMSFNLTNIKRLVGMvwpMTPDQLVNLTNQG 268
Cdd:cd07206 246 --TIIPPFSFSNPLKLLSN---PSEDELQRLILEG 275
 
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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