NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|156363885|ref|XP_001626270|]
View 

patatin-like phospholipase domain-containing protein 4 [Nematostella vectensis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2-241 6.91e-106

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 cd07222:

Pssm-ID: 416256 [Multi-domain]  Cd Length: 246  Bit Score: 306.18  E-value: 6.91e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATsVP--LEQCSHFVQDLAKEARKKPLGPINP 79
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLT-APekIEECKEFTYKFAEEVRKQRFGAMTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  80 EFDLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYD 159
Cdd:cd07222   80 GYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 160 GGFTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAV 239
Cdd:cd07222  160 GGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                 ..
gi 156363885 240 NY 241
Cdd:cd07222  240 RF 241
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 2-241 6.91e-106

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: 306.18  E-value: 6.91e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATsVP--LEQCSHFVQDLAKEARKKPLGPINP 79
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLT-APekIEECKEFTYKFAEEVRKQRFGAMTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  80 EFDLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYD 159
Cdd:cd07222   80 GYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 160 GGFTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAV 239
Cdd:cd07222  160 GGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                 ..
gi 156363885 240 NY 241
Cdd:cd07222  240 RF 241
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 3-167 1.61e-22

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: 91.13  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885    3 LSFAGCGFLGVYHLGVAAGLSKSAPRFlksiEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKE------------AR 70
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRF----DVISGTSAGAINAALLALGRDPEEIEDLLLELDLNlflslirkralsLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   71 KKPLGPINP-EFDLIGYLRGGLEKFLPHDGHEMATGRL-----------YVSVTRLKDNRNVLLSQYD--SREFLIETLL 136
Cdd:pfam01734  77 ALLRGLIGEgGLFDGDALRELLRKLLGDLTLEELAARLslllvvalralLTVISTALGTRARILLPDDldDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 156363885  137 ASCFIPIYagLKFPQFDGQKWYDGGFTDNLP 167
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVP 185
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 2-238 1.18e-19

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 84.95  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRflksIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPEF 81
Cdd:COG1752    8 GLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRRLLR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  82 DLIGYLRGG----------LEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDsrefLIETLLASCFIPIYaglkFP- 150
Cdd:COG1752   84 LDLGLSPGGlldgdplrrlLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGP----LADAVRASAAIPGV----FPp 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 151 -QFDGQKWYDGGFTDNLP----RPPHGKTILVSPFSGDSDICP------EDSSRVMaefkwrnMSVSLNKDNAMRTQHIL 219
Cdd:COG1752  156 vEIDGRLYVDGGVVNNLPvdpaRALGADRVIAVDLNPPLRKLPslldilGRALEIM-------FNSILRRELALEPADIL 228

                        250       260
                 ....*....|....*....|....*..
gi 156363885 220 YPPNQQAF--------DKLYQAGYKDA 238
Cdd:COG1752  229 IEPDLSGIslldfsraEELIEAGYEAA 255
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 2-241 6.91e-106

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: 306.18  E-value: 6.91e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATsVP--LEQCSHFVQDLAKEARKKPLGPINP 79
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLT-APekIEECKEFTYKFAEEVRKQRFGAMTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  80 EFDLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYD 159
Cdd:cd07222   80 GYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 160 GGFTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAV 239
Cdd:cd07222  160 GGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                 ..
gi 156363885 240 NY 241
Cdd:cd07222  240 RF 241
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 2-241 6.38e-105

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: 303.50  E-value: 6.38e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPEF 81
Cdd:cd07204    1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  82 DLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYDGG 161
Cdd:cd07204   81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 162 FTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAVNY 241
Cdd:cd07204  161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 1-247 1.98e-96

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: 282.31  E-value: 1.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   1 MNLSFAGCGFLGVYHLGVAAGLSKSAPRFLksIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPE 80
Cdd:cd07218    1 MNLSFAGCGFLGIYHVGVAVCLKKYAPHLL--LNKISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  81 FDLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYDG 160
Cdd:cd07218   79 FNIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 161 GFTDNLPRpPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAVN 240
Cdd:cd07218  159 GFSDNLPT-LDENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALR 237


                 ....*..
gi 156363885 241 YVTTKGL 247
Cdd:cd07218  238 FLHRNNL 244
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 1-242 9.95e-96

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: 280.48  E-value: 9.95e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   1 MNLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPE 80
Cdd:cd07220    5 WNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGPLHPS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  81 FDLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYDG 160
Cdd:cd07220   85 FNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRYVDG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 161 GFTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAVN 240
Cdd:cd07220  165 GISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRDALR 244


                 ..
gi 156363885 241 YV 242
Cdd:cd07220  245 FL 246
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 2-247 7.71e-67

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: 207.32  E-value: 7.71e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPEF 81
Cdd:cd07221    2 SLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPSF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  82 DLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYDGG 161
Cdd:cd07221   82 NLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 162 FTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAVNY 241
Cdd:cd07221  162 VSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFRF 241


                 ....*.
gi 156363885 242 VTTKGL 247
Cdd:cd07221  242 LEENGI 247
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 2-242 9.18e-66

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: 208.59  E-value: 9.18e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPEF 81
Cdd:cd07219   14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  82 DLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYDGG 161
Cdd:cd07219   94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 162 FTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAVNY 241
Cdd:cd07219  174 FTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLY 253


                 .
gi 156363885 242 V 242
Cdd:cd07219  254 L 254
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 2-248 3.97e-50

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: 168.94  E-value: 3.97e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPEF 81
Cdd:cd07223   11 NLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIFHPAY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  82 DLIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYDGG 161
Cdd:cd07223   91 APIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDGA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 162 FTDNLPRPPHGKTILVSPFSGDSDICPEDSSRVMAEFKWRNMSVSLNKDNAMRTQHILYPPNQQAFDKLYQAGYKDAVNY 241
Cdd:cd07223  171 LSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLDALRF 250


                 ....*..
gi 156363885 242 VTTKGLS 248
Cdd:cd07223  251 LERRGLT 257
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 3-179 5.82e-50

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: 161.36  E-value: 5.82e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLGVAAGLSKSAPRflksIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPEFD 82
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  83 LIGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQyDSREFLIETLLASCFIPIYAGLKFPQFDGQKWYDGGF 162
Cdd:cd07198   77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVSD-TSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                        170
                 ....*....|....*..
gi 156363885 163 TDNLPRPPHGKTILVSP 179
Cdd:cd07198  156 SNNLPVAELGNTINVSP 172
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 4-238 9.05e-38

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: 132.08  E-value: 9.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   4 SFAGCGFLGVYHLGVAAGLSKSAprFLKSIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKplgpiNPEFDL 83
Cdd:cd07224    3 SFSAAGLLFPYHLGVLSLLIEAG--VINETTPLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSN-----GTAFRL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  84 IGYLRGGLEKFLPHDGHE-MATGRLYVSVTRLKDN-RNVLLSQYDSREFLIETLLASCFIPIY-AGLKFPQFDGQKWYDG 160
Cdd:cd07224   76 GGVLRDELDKTLPDDAHErCNRGRIRVAVTQLFPVpRGLLVSSFDSKSDLIDALLASCNIPGYlAPWPATMFRGKLCVDG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 161 GFTDNLPRP-PHGKTILVSPFSGDS------DICPEDSSRVMAefkwrNMSVSLNKDnamrtqhiLYPPNQQAFDKLYQA 233
Cdd:cd07224  156 GFALFIPPTtAADRTVRVCPFPASRssikgqNLDNDDTEDVPY-----SRRQLLNWA--------LEPADDAMLLELFNE 222


                 ....*
gi 156363885 234 GYKDA 238
Cdd:cd07224  223 GYKDA 227
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 3-179 2.44e-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: 102.49  E-value: 2.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLGVAAGLSKSAPrfLKSIEAFAGASAGSLIAAALatsvpleqcshfvqdlakearkkplgpINPEFD 82
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGL--LDCVTYLAGTSGGAWVAATL---------------------------YPPSSS 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  83 LIGYLRGGLEkflphdghEMATGRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAGLKFPQ----------F 152
Cdd:cd01819   52 LDNKPRQSLE--------EALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPAelytsksnlkE 123

                        170       180       190
                 ....*....|....*....|....*....|..
gi 156363885 153 DGQKWYDGGFTDNLP-----RPPHGKTILVSP 179
Cdd:cd01819  124 KGVRLVDGGVSNNLPapvllRPGRGVTLTISP 155
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 3-167 1.61e-22

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: 91.13  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885    3 LSFAGCGFLGVYHLGVAAGLSKSAPRFlksiEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKE------------AR 70
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIRF----DVISGTSAGAINAALLALGRDPEEIEDLLLELDLNlflslirkralsLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   71 KKPLGPINP-EFDLIGYLRGGLEKFLPHDGHEMATGRL-----------YVSVTRLKDNRNVLLSQYD--SREFLIETLL 136
Cdd:pfam01734  77 ALLRGLIGEgGLFDGDALRELLRKLLGDLTLEELAARLslllvvalralLTVISTALGTRARILLPDDldDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 156363885  137 ASCFIPIYagLKFPQFDGQKWYDGGFTDNLP 167
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVP 185
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 2-238 1.18e-19

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 84.95  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAPRflksIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINPEF 81
Cdd:COG1752    8 GLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLSLPRRLLR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  82 DLIGYLRGG----------LEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDsrefLIETLLASCFIPIYaglkFP- 150
Cdd:COG1752   84 LDLGLSPGGlldgdplrrlLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGP----LADAVRASAAIPGV----FPp 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 151 -QFDGQKWYDGGFTDNLP----RPPHGKTILVSPFSGDSDICP------EDSSRVMaefkwrnMSVSLNKDNAMRTQHIL 219
Cdd:COG1752  156 vEIDGRLYVDGGVVNNLPvdpaRALGADRVIAVDLNPPLRKLPslldilGRALEIM-------FNSILRRELALEPADIL 228

                        250       260
                 ....*....|....*....|....*..
gi 156363885 220 YPPNQQAF--------DKLYQAGYKDA 238
Cdd:COG1752  229 IEPDLSGIslldfsraEELIEAGYEAA 255
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 2-178 1.57e-17

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: 78.54  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKS--APRflksieAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKKPLGPINP 79
Cdd:cd07210    2 ALVLSSGFFGFYAHLGFLAALLEMglEPS------AISGTSAGALVGGLFASGISPDEMAELLLSLERKDFWMFWDPPLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  80 efdlIGYLRGG-----LEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDsrefLIETLLASCFIPiyaGLKFPQ-FD 153
Cdd:cd07210   76 ----GGLLSGDrfaalLREHLPPDRFEELRIPLAVSVVDLTSRETLLLSEGD----LAEAVAASCAVP---PLFQPVeIG 144

                        170       180
                 ....*....|....*....|....*....
gi 156363885 154 GQKWYDGGFTDNLP----RPPHGKTILVS 178
Cdd:cd07210  145 GRPFVDGGVADRLPfdalRPEIERILYHH 173
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 3-167 7.10e-13

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: 65.39  E-value: 7.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLGVAAGLsksAPRFLKsIEAFAGASAGSLIAAALAT--SVPLEQCSHFVQDLAKEArkkplgpinpe 80
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKAL---AEAGIE-PDIISGTSIGAINGALIAGgdPEAVERLEKLWRELSRED----------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  81 fdliGYLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDS--REFLIETLLASCFIPIYaglkFP--QFDGQK 156
Cdd:cd07209   66 ----VFLRGLLDRALDFDTLRLLAILFAGLVIVAVNVLTGEPVYFDDipDGILPEHLLASAALPPF----FPpvEIDGRY 137

                        170
                 ....*....|.
gi 156363885 157 WYDGGFTDNLP 167
Cdd:cd07209  138 YWDGGVVDNTP 148
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 3-167 1.20e-09

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: 55.63  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLGVAAGLSKSAPRflksIEAFAGASAGSLIAAALATSVPLEQCSHFVQdLAKEARKKPLGPINPEFD 82
Cdd:cd07205    3 LALSGGGARGLAHIGVLKALEEAGIP----IDIVSGTSAGAIVGALYAAGYSPEEIEERAK-LRSTDLKALSDLTIPTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  83 LIG--YLRGGLEKFLPHDGHEMATGRLYVSVTRLKDNRNVLLSQYDsrefLIETLLASCFIPIYaglkFPQF--DGQKWY 158
Cdd:cd07205   78 LLRgdKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFRSGS----LVRAVRASMSIPGI----FPPVkiDGQLLV 149


                 ....*....
gi 156363885 159 DGGFTDNLP 167
Cdd:cd07205  150 DGGVLNNLP 158
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
33-167 1.98e-08

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 53.63  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  33 IEAFAGASAGSLIAAALATSVPLEQCsHFVQDLAKearkkplgpiNPEF-DLIGYLRGG------------LEKFLPHDG 99
Cdd:COG4667   34 FDLVIGVSAGALNGASYLSRQPGRAR-RVITDYAT----------DPRFfSLRNFLRGGnlfdldflydeiPNELLPFDF 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885 100 HEMATG--RLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAglKFPQFDGQKWYDGGFTDNLP 167
Cdd:COG4667  103 ETFKASprEFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLY--PPVEIDGKRYLDGGVADSIP 170
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 2-167 3.08e-08

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: 52.28  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   2 NLSFAGCGFLGVYHLGVAAGLSKSAprflKSIEAFAGASAGSLIAAALATSVPLEQcshfVQDLAKEARKKPL--GPINP 79
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKALEEAG----ILKKRVAGTSAGAITAALLALGYSAAD----IKDILKETDFAKLldSPVGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  80 EFDLIGYLRGG-------LEKFL-------------PHDGHEMATGR---LYVSVTRLKDNRNVLLSQYDSREFLI-ETL 135
Cdd:cd07207   73 LFLLPSLFKEGglykgdaLEEWLrellkektgnsfaTSLLRDLDDDLgkdLKVVATDLTTGALVVFSAETTPDMPVaKAV 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 156363885 136 LASCFIPIYagLKFPQFD-GQKWYDGGFTDNLP 167
Cdd:cd07207  153 RASMSIPFV--FKPVRLAkGDVYVDGGVLDNYP 183
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 3-72 4.15e-08

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: 52.68  E-value: 4.15e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLGVAAGLSKSAPRFLKSIEAFAGASAGSLIAAALATSVPLEQCSHFVQDLAKEARKK 72
Cdd:cd07213    5 LSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIDLFAGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSK 74
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 105-167 1.56e-06

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: 47.99  E-value: 1.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156363885 105 GRLYVSVTRLKDNRNVLLSQYDSREFLIETLLASCFIPIYAglKFPQFDGQKWYDGGFTDNLP 167
Cdd:cd07208  104 ARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLF--PPVRIDGEPYVDGGLSDSIP 164
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 3-167 3.02e-06

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: 47.21  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLGVAAGLSKSA--PRFLksieafAGASAGSLIAAALATSVPLEqcshFVQDLA-KEARKKplgpinp 79
Cdd:cd07206   72 LMLSGGASLGLFHLGVVKALWEQDllPRVI------SGSSAGAIVAALLGTHTDEE----LIGDLTfQEAYER------- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  80 efdligylrgglekflphdghemaTGR-LYVSVTRLKDNRN-VLLSQYDSREFLI-ETLLASCFIP-IY----------A 145
Cdd:cd07206  135 ------------------------TGRiINITVAPAEPHQNsRLLNALTSPNVLIwSAVLASCAVPgVFppvmlmaknrD 190

                        170       180
                 ....*....|....*....|..
gi 156363885 146 GLKFPQFDGQKWYDGGFTDNLP 167
Cdd:cd07206  191 GEIVPYLPGRKWVDGSVSDDLP 212
Pat17_PNPLA8_PNPLA9_like cd07199
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ...
 3-167 1.47e-04

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: 41.93  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLgvaaglsksapRFLKSIEA--------------FAGASAGSLIAAALATS-VPLEQCSHFVQDLAK 67
Cdd:cd07199    2 LSLDGGGIRGIIPA-----------EILAELEKrlgkpsriadlfdlIAGTSTGGIIALGLALGrYSAEELVELYEELGR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  68 earkkplgpinpefdligylrgglEKFlphdghematGRLYVSVTRLKDNRNVLLSQYDSREF-------LIETLLASCF 140
Cdd:cd07199   71 ------------------------KIF----------PRVLVTAYDLSTGKPVVFSNYDAEEPdddddfkLWDVARATSA 116

                        170       180
                 ....*....|....*....|....*....
gi 156363885 141 IPIY-AGLKFPQFDGQKWY-DGGFTDNLP 167
Cdd:cd07199  117 APTYfPPAVIESGGDEGAFvDGGVAANNP 145
Pat_PLPL cd07232
Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin ...
 3-167 1.96e-04

Patain-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants and fungi. 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 been found also in vertebrates.


Pssm-ID: 132870  Cd Length: 407  Bit Score: 41.87  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885   3 LSFAGCGFLGVYHLGVAAGLSKSapRFLKSIeaFAGASAGSLIAAALATSVPLEQCSHFVQDLAKeaRKKPLGPINPE-- 80
Cdd:cd07232   70 LCLSGGAAFAYYHFGVVKALLDA--DLLPNV--ISGTSGGSLVAALLCTRTDEELKQLLVPELAR--KITACEPPWLVwi 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156363885  81 ---------FDLIGYLRgGLEKFLPHD-----GHEMaTGR-LYVSVTRLKDNRNVLLSQY-DSREFLI-ETLLASCFIP- 142
Cdd:cd07232  144 prwlktgarFDSVEWAR-TCCWFTRGSmtfeeAYER-TGRiLNISVVPADPHSPTILLNYlTSPNCTIwSAVLASAAVPg 221

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 156363885 143 IYA-----------GLKFPQFDGQKWYDGGFTDNLP 167
Cdd:cd07232  222 ILNpvvlmmkdpdgTLIPPFSFGSKWKDGSLRTDIP 257
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 3-65 2.21e-04

Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This acyl-hydrolase domain is homologus to yeast triacylglycerol lipase 3 and human adipose triglyceride lipase. This family includes SDP1 from Arabidopsis thaliana.


Pssm-ID: 132869  Cd Length: 323  Bit Score: 41.67  E-value: 2.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156363885   3 LSFAGCGFLGVYHLGVAAGL--SKSAPRFLksieafAGASAGSLIAAALATSVPlEQCSHFVQDL 65
Cdd:cd07231   71 LLLSGGAALGTFHVGVVRTLveHQLLPRVI------AGSSVGSIVCAIIATRTD-EELQSFFRAL 128
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH