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Conserved domains on  [gi|25148968|ref|NP_741195|]
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PNPLA domain-containing protein [Caenorhabditis elegans]

Protein Classification

patatin-like phospholipase domain-containing protein; patatin-like phospholipase family protein( domain architecture ID 10163305)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 12-252 3.10e-146

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: 427.54  E-value: 3.10e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEF 89
Cdd:cd07204   1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNarRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  90 NLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGG 169
Cdd:cd07204  81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 170 VSDNQPIY-DEHTVTVSPFSGESDICPPDWDSGSMLgVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALR 248
Cdd:cd07204 161 LSDNLPILdDENTITVSPFSGESDICPQDKSSNLLE-VNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALR 239


                ....
gi 25148968 249 FLTK 252
Cdd:cd07204 240 FLER 243
 
Name Accession Description Interval E-value
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 12-252 3.10e-146

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: 427.54  E-value: 3.10e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEF 89
Cdd:cd07204   1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNarRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  90 NLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGG 169
Cdd:cd07204  81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 170 VSDNQPIY-DEHTVTVSPFSGESDICPPDWDSGSMLgVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALR 248
Cdd:cd07204 161 LSDNLPILdDENTITVSPFSGESDICPQDKSSNLLE-VNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALR 239


                ....
gi 25148968 249 FLTK 252
Cdd:cd07204 240 FLER 243
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 13-176 3.23e-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: 89.21  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968    13 LSFSGCGFLCVYHAGVAAAIKE--YAPELlqnkILGASAGSIVACGLITGVCISHATSTILKVVSQAR-SRTFGPLHPEF 89
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEagIRFDV----ISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFlSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968    90 NLL------------GIVRDELEVILPPNAYEMCTGRL-------------VISLTRWSDHENVIIDEYRSNADLIDAIM 144
Cdd:pfam01734  77 ALLrgligegglfdgDALRELLRKLLGDLTLEELAARLslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 25148968   145 CSCFIPLYcgITPPKFRGVQYIDGGVSDNQPI 176
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 12-176 1.32e-12

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 68.39  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKE--YAPELlqnkILGASAGSIVACGLITG--------VCISHATSTILKVVSQARSRT 81
Cdd:COG1752   8 GLVLSGGGARGAAHIGVLKALEEagIPPDV----IAGTSAGAIVGALYAAGysadeleeLWRSLDRRDLFDLSLPRRLLR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  82 FGPLHPEFNLLGI--VRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDeyrsNADLIDAIMCSCFIPlycGITPP- 158
Cdd:COG1752  84 LDLGLSPGGLLDGdpLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAAIP---GVFPPv 156

                       170
                ....*....|....*...
gi 25148968 159 KFRGVQYIDGGVSDNQPI 176
Cdd:COG1752 157 EIDGRLYVDGGVVNNLPV 174
 
Name Accession Description Interval E-value
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 12-252 3.10e-146

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: 427.54  E-value: 3.10e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEF 89
Cdd:cd07204   1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNarRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  90 NLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGG 169
Cdd:cd07204  81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 170 VSDNQPIY-DEHTVTVSPFSGESDICPPDWDSGSMLgVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALR 248
Cdd:cd07204 161 LSDNLPILdDENTITVSPFSGESDICPQDKSSNLLE-VNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALR 239


                ....
gi 25148968 249 FLTK 252
Cdd:cd07204 240 FLER 243
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 11-255 2.38e-109

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: 332.39  E-value: 2.38e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  11 MNLSFSGCGFLCVYHAGVAAAIKEYAPELLQNKILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEFN 90
Cdd:cd07218   1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSFN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  91 LLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGGV 170
Cdd:cd07218  81 IQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGGF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 171 SDNQPIYDEHTVTVSPFSGESDICPPDwDSGSMLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALRFL 250
Cdd:cd07218 161 SDNLPTLDENTITVSPFCGESDICPRD-NSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRFL 239


                ....*
gi 25148968 251 TKCGL 255
Cdd:cd07218 240 HRNNL 244
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 11-252 4.04e-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: 316.69  E-value: 4.04e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  11 MNLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPE 88
Cdd:cd07220   5 WNISFAGCGFLGVYHVGVASCLLEHAPFLVANarKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPLHPS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  89 FNLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDG 168
Cdd:cd07220  85 FNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRYVDG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 169 GVSDNQPIYD-EHTVTVSPFSGESDICPPDwDSGSMLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDAL 247
Cdd:cd07220 165 GISDNLPQYElKNTITVSPFSGESDICPRD-SSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRDAL 243


                ....*
gi 25148968 248 RFLTK 252
Cdd:cd07220 244 RFLKE 248
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 12-255 9.77e-82

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: 260.86  E-value: 9.77e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEF 89
Cdd:cd07221   2 SLSFAGCGFLGFYHVGVTRCLSERAPHLLRDarMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  90 NLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGG 169
Cdd:cd07221  82 NLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDGG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 170 VSDNQPIYD-EHTVTVSPFSGESDICpPDWDSGSMLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALR 248
Cdd:cd07221 162 VSDNVPFFDaKTTITVSPFYGEYDIC-PKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240


                ....*..
gi 25148968 249 FLTKCGL 255
Cdd:cd07221 241 FLEENGI 247
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 12-252 2.13e-62

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 213.99  E-value: 2.13e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEF 89
Cdd:cd07219  14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETahRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  90 NLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGG 169
Cdd:cd07219  94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 170 VSDNQPI-YDEHTVTVSPFSGESDICPPDWDSGSMLGVDFNGtSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALR 248
Cdd:cd07219 174 FTGMQPCsFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNC-SFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVL 252


                ....
gi 25148968 249 FLTK 252
Cdd:cd07219 253 YLRR 256
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 12-252 3.56e-61

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: 206.03  E-value: 3.56e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGV-CISHATSTILKVVSQARSRTFGPLHPE 88
Cdd:cd07222   1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRvkRFAGASAGSLVAAVLLTAPeKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  89 FNLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDG 168
Cdd:cd07222  81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 169 GVSDNQPIY-DEHTVTVSPFSGESDICPPDWDSGSmLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDAL 247
Cdd:cd07222 161 GFTNSLPVLpVGRTITVSPFSGRADICPQDKGQLD-LYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                ....*
gi 25148968 248 RFLTK 252
Cdd:cd07222 240 RFLKK 244
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 12-255 1.01e-60

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: 210.15  E-value: 1.01e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELLQN--KILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEF 89
Cdd:cd07223  11 NLSFSGAGYLGLYHVGVTECLRQRAPRLLQGarRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIFHPAY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  90 NLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGG 169
Cdd:cd07223  91 APIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDGA 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 170 VSDNQPIYD-EHTVTVSPFSGESDICPPDwDSGSMLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALR 248
Cdd:cd07223 171 LSNNLPFSDcPSTITVSPFHGTVDICPQS-TSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLDALR 249


                ....*..
gi 25148968 249 FLTKCGL 255
Cdd:cd07223 250 FLERRGL 256
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 13-186 4.21e-48

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: 167.52  E-value: 4.21e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAIKEYAPELlqNKILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEFNLL 92
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRERGPLI--DIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGRLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  93 GIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEyRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGGVSD 172
Cdd:cd07198  79 GILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVSD-TSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGLSN 157

                       170
                ....*....|....*
gi 25148968 173 NQPIYD-EHTVTVSP 186
Cdd:cd07198 158 NLPVAElGNTINVSP 172
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 14-250 1.32e-31

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: 123.22  E-value: 1.32e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  14 SFSGCGFLCVYHAGVAA------AIKEYAPellqnkILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTfgplhP 87
Cdd:cd07224   3 SFSAAGLLFPYHLGVLSllieagVINETTP------LAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNG-----T 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  88 EFNLLGIVRDELEVILPPNAYEMC-TGRLVISLTR-WSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPP-KFRGVQ 164
Cdd:cd07224  72 AFRLGGVLRDELDKTLPDDAHERCnRGRIRVAVTQlFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLAPWPAtMFRGKL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968 165 YIDGGVSDNQPIYD--EHTVTVSPFsgesdicPPDWDSGSMLGVDFNGTS-IRFTTRNMFRLmaCLWPRSTDDLSRMCLQ 241
Cdd:cd07224 152 CVDGGFALFIPPTTaaDRTVRVCPF-------PASRSSIKGQNLDNDDTEdVPYSRRQLLNW--ALEPADDAMLLELFNE 222


                ....*....
gi 25148968 242 GFGDALRFL 250
Cdd:cd07224 223 GYKDANEWA 231
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 13-186 8.21e-27

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: 106.73  E-value: 8.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAIKEYAPELLQNKILGASAGSIVACGLitgvcishatstilkvvsqarsrtfgpLHPEFNLL 92
Cdd:cd01819   1 LSFSGGGFRGMYHAGVLSALAERGLLDCVTYLAGTSGGAWVAATL---------------------------YPPSSSLD 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  93 GIVRDELEVILppnayemcTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPP----------KFRG 162
Cdd:cd01819  54 NKPRQSLEEAL--------SGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKEKG 125

                       170       180       190
                ....*....|....*....|....*....|
gi 25148968 163 VQYIDGGVSDNQPIY------DEHTVTVSP 186
Cdd:cd01819 126 VRLVDGGVSNNLPAPvllrpgRGVTLTISP 155
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 13-176 3.23e-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: 89.21  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968    13 LSFSGCGFLCVYHAGVAAAIKE--YAPELlqnkILGASAGSIVACGLITGVCISHATSTILKVVSQAR-SRTFGPLHPEF 89
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEagIRFDV----ISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFlSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968    90 NLL------------GIVRDELEVILPPNAYEMCTGRL-------------VISLTRWSDHENVIIDEYRSNADLIDAIM 144
Cdd:pfam01734  77 ALLrgligegglfdgDALRELLRKLLGDLTLEELAARLslllvvalralltVISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 25148968   145 CSCFIPLYcgITPPKFRGVQYIDGGVSDNQPI 176
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPV 186
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 12-176 1.32e-12

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 68.39  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKE--YAPELlqnkILGASAGSIVACGLITG--------VCISHATSTILKVVSQARSRT 81
Cdd:COG1752   8 GLVLSGGGARGAAHIGVLKALEEagIPPDV----IAGTSAGAIVGALYAAGysadeleeLWRSLDRRDLFDLSLPRRLLR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  82 FGPLHPEFNLLGI--VRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDeyrsNADLIDAIMCSCFIPlycGITPP- 158
Cdd:COG1752  84 LDLGLSPGGLLDGdpLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAAIP---GVFPPv 156

                       170
                ....*....|....*...
gi 25148968 159 KFRGVQYIDGGVSDNQPI 176
Cdd:COG1752 157 EIDGRLYVDGGVVNNLPV 174
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 12-185 3.85e-12

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: 66.22  E-value: 3.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  12 NLSFSGCGFLCVYHAGVAAAIKEYAPELlqNKILGASAGSIV----ACGLITGVCISHatstilkVVSQARSRTFGPLHP 87
Cdd:cd07210   2 ALVLSSGFFGFYAHLGFLAALLEMGLEP--SAISGTSAGALVgglfASGISPDEMAEL-------LLSLERKDFWMFWDP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  88 EfNLLGI-----VRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEyrsnADLIDAIMCSCFIP-LYCgitPPKFR 161
Cdd:cd07210  73 P-LRGGLlsgdrFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSE----GDLAEAVAASCAVPpLFQ---PVEIG 144

                       170       180
                ....*....|....*....|....*..
gi 25148968 162 GVQYIDGGVSDNQPI---YDEHTVTVS 185
Cdd:cd07210 145 GRPFVDGGVADRLPFdalRPEIERILY 171
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
15-182 8.42e-12

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 66.34  E-value: 8.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  15 FSGCGFLCVYHAGVAAAikeyapeLLQNKI-----LGASAGSIVACGLITGVcISHATSTILKVVsqARSRTFGPLHpeF 89
Cdd:COG4667  10 LEGGGMRGIFTAGVLDA-------LLEEGIpfdlvIGVSAGALNGASYLSRQ-PGRARRVITDYA--TDPRFFSLRN--F 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  90 ----NLLGI--VRDELEVILPPNAYEM---CTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGitPPKF 160
Cdd:COG4667  78 lrggNLFDLdfLYDEIPNELLPFDFETfkaSPREFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP--PVEI 155

                       170       180
                ....*....|....*....|....*....
gi 25148968 161 RGVQYIDGGVSDNQPI-------YDEHTV 182
Cdd:COG4667 156 DGKRYLDGGVADSIPVreairdgADKIVV 184
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 13-176 3.13e-11

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: 64.55  E-value: 3.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAikeyapeLLQNKI------LGASAGSIVACGLITG-------VCISHATSTilkvvsqars 79
Cdd:cd07208   1 LVLEGGGMRGAYTAGVLDA-------FLEAGIrpfdlvIGVSAGALNAASYLSGqrgralrINTKYATDP---------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  80 RTFGP-----LHPEFNLLGIVrDELEVILPP---NAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPL 151
Cdd:cd07208  64 RYLGLrsllrTGNLFDLDFLY-DELPDGLDPfdfEAFAASPARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPG 142

                       170       180
                ....*....|....*....|....*
gi 25148968 152 YCGitPPKFRGVQYIDGGVSDNQPI 176
Cdd:cd07208 143 LFP--PVRIDGEPYVDGGLSDSIPV 165
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 13-176 1.68e-08

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


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 54.86  E-value: 1.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAIKEYapELLQNKILGASAGSIVAcGLItgvCISHATSTILKVVSQARSRTFGPLHPEFNLL 92
Cdd:cd07205   3 LALSGGGARGLAHIGVLKALEEA--GIPIDIVSGTSAGAIVG-ALY---AAGYSPEEIEERAKLRSTDLKALSDLTIPTA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  93 GIVR-----------------DELEVILPPNAYEMCTGRLVISltrwsdhenviideyrSNADLIDAIMCSCFIPlycGI 155
Cdd:cd07205  77 GLLRgdkflelldeyfgdrdiEDLWIPFFIVATDLTSGKLVVF----------------RSGSLVRAVRASMSIP---GI 137

                       170       180
                ....*....|....*....|..
gi 25148968 156 TPP-KFRGVQYIDGGVSDNQPI 176
Cdd:cd07205 138 FPPvKIDGQLLVDGGVLNNLPV 159
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 7-176 3.68e-07

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: 52.60  E-value: 3.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968   7 RPELMnlsFSGCGFLCVYHAGVAAAIKEYapELLQNKILGASAGSIVAcglitgvcishatstilkvvsqarsrtfgplh 86
Cdd:cd07206  69 RTALM---LSGGASLGLFHLGVVKALWEQ--DLLPRVISGSSAGAIVA-------------------------------- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  87 pefNLLGIVRDElEVIlpPN-----AYEMcTGRLV-ISLTRWSDHENVIIDEYRSNADLI--DAIMCSCFIP-------L 151
Cdd:cd07206 112 ---ALLGTHTDE-ELI--GDltfqeAYER-TGRIInITVAPAEPHQNSRLLNALTSPNVLiwSAVLASCAVPgvfppvmL 184

                       170       180
                ....*....|....*....|....*....
gi 25148968 152 YC----GITPPKFRGVQYIDGGVSDNQPI 176
Cdd:cd07206 185 MAknrdGEIVPYLPGRKWVDGSVSDDLPA 213
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 13-175 2.36e-06

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 subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132852 [Multi-domain]  Cd Length: 288  Bit Score: 49.98  E-value: 2.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAIKEYAPELLQNK--ILGASAGSIVACGLITGVCISHATSTILKVVSQARSRT---FGPLHP 87
Cdd:cd07213   5 LSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIdlFAGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSKSsagGGAGNN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  88 EFNLLGIVRDELEVILPPNAYEMCTGRLVI-----------SLTRW-SDHENVIIDEYRSNADLIDAIMCSCFIPLYcgi 155
Cdd:cd07213  85 QYFAAGFLKAFAEVFFGDLTLGDLKRKVLVpsfqldsgkddPNRRWkPKLFHNFPGEPDLDELLVDVCLRSSAAPTY--- 161

                       170       180
                ....*....|....*....|.
gi 25148968 156 tppkFRGVQ-YIDGGVSDNQP 175
Cdd:cd07213 162 ----FPSYQgYVDGGVFANNP 178
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 13-176 1.08e-05

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: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAIKE--YAPELlqnkILGASAGSI----VACGLITGV--------CISHATSTILKVVSQAr 78
Cdd:cd07209   1 LVLSGGGALGAYQAGVLKALAEagIEPDI----ISGTSIGAIngalIAGGDPEAVerleklwrELSREDVFLRGLLDRA- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  79 srtfgPLHPEFNLLGIvrdeLEVILPPNAYEMCTGrlvisltrwsdhENVIIDEyRSNADLIDAIMCSCFIPLycGITPP 158
Cdd:cd07209  76 -----LDFDTLRLLAI----LFAGLVIVAVNVLTG------------EPVYFDD-IPDGILPEHLLASAALPP--FFPPV 131

                       170
                ....*....|....*...
gi 25148968 159 KFRGVQYIDGGVSDNQPI 176
Cdd:cd07209 132 EIDGRYYWDGGVVDNTPL 149
PATA COG3621
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ...
 13-175 2.37e-05

Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];


Pssm-ID: 442839 [Multi-domain]  Cd Length: 296  Bit Score: 46.82  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAIKEYapelLQNKIL-------GASAGSIVACGLITGVCISHatstILKVVSQARSRTFGPL 85
Cdd:COG3621  10 LSLDGGGIRGLIPARILAELEER----LGKPLAeyfdliaGTSTGGIIALGLAAGYSAEE----ILDLYEEEGKEIFPKS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  86 HPE--FNLLGIV---------RDELEVILPPNAYEMCTGRLVI---SLTRWS-------DHENVIIDEYRsnadLIDAIM 144
Cdd:COG3621  82 RWRklLSLRGLFgpkydseglEKVLKEYFGDTTLGDLKTPVLIpsyDLDNGKpvffkspHAKFDRDRDFL----LVDVAR 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 25148968 145 CSCFIPLY---CGITPPKFRGVQYIDGGVSDNQP 175
Cdd:COG3621 158 ATSAAPTYfppAQIKNLTGEGYALIDGGVFANNP 191
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 13-176 7.94e-03

Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; 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 subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.


Pssm-ID: 132838 [Multi-domain]  Cd Length: 258  Bit Score: 38.85  E-value: 7.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  13 LSFSGCGFLCVYHAGVAAAIkEyapELLQNK---------ILGASAGSIVACGLITGVcisHATSTILKVVSQARSRTFG 83
Cdd:cd07199   2 LSLDGGGIRGIIPAEILAEL-E---KRLGKPsriadlfdlIAGTSTGGIIALGLALGR---YSAEELVELYEELGRKIFP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25148968  84 PlhpefnllgivrdeleVILPpnAYEMCTGRLVIsLTRWSDHENVIIDEYRsnadLIDAIMCSCFIPLYcgiTPPK---- 159
Cdd:cd07199  75 R----------------VLVT--AYDLSTGKPVV-FSNYDAEEPDDDDDFK----LWDVARATSAAPTY---FPPAvies 128

                       170
                ....*....|....*...
gi 25148968 160 -FRGVQYIDGGVSDNQPI 176
Cdd:cd07199 129 gGDEGAFVDGGVAANNPA 146
 
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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