NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2266238920|ref|XP_048784563|]
View 

patatin-like phospholipase domain-containing protein 4 isoform X5 [Lagopus muta]

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 ...
 31-197 1.79e-111

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: 318.12  E-value: 1.79e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  31 GSSCSLQAWEGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVD 110
Cdd:cd07222    80 GYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWID 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920 111 GGITNGLPILPFGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAV 190
Cdd:cd07222   160 GGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                  ....*..
gi 2266238920 191 HFLLKEN 197
Cdd:cd07222   240 RFLKKEN 246
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 31-197 1.79e-111

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: 318.12  E-value: 1.79e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  31 GSSCSLQAWEGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVD 110
Cdd:cd07222    80 GYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWID 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920 111 GGITNGLPILPFGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAV 190
Cdd:cd07222   160 GGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                  ....*..
gi 2266238920 191 HFLLKEN 197
Cdd:cd07222   240 RFLKKEN 246
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
43-119 2.96e-12

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 63.65  E-value: 2.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2266238920  43 ESILPSNAHEIAEN--RLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYagMKPVEYKGEKWVDGGITNGLPI 119
Cdd:COG4667    95 NELLPFDFETFKASprEFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLL--YPPVEIDGKRYLDGGVADSIPV 171
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 62-122 9.68e-10

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: 55.69  E-value: 9.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2266238920  62 VTNVRNGKNYLFS-NFASREDLIKVLLASSFIPVYagMKPVEYKGEKWVDGGITNGLPILPF 122
Cdd:pfam01734 130 STALGTRARILLPdDLDDDEDLADAVLASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 31-197 1.79e-111

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: 318.12  E-value: 1.79e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  31 GSSCSLQAWEGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVD 110
Cdd:cd07222    80 GYDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWID 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920 111 GGITNGLPILPFGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAV 190
Cdd:cd07222   160 GGFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                  ....*..
gi 2266238920 191 HFLLKEN 197
Cdd:cd07222   240 RFLKKEN 246
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 40-195 5.37e-77

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: 230.70  E-value: 5.37e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  40 EGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVDGGITNGLPI 119
Cdd:cd07204    88 QGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGGLSDNLPI 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2266238920 120 LPFGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAVHFLLK 195
Cdd:cd07204   168 LDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRFLER 243
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 40-197 1.22e-55

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: 176.38  E-value: 1.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  40 EGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVDGGITNGLPI 119
Cdd:cd07218    87 EGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGGFSDNLPT 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266238920 120 LPfGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAVHFLLKEN 197
Cdd:cd07218   167 LD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRFLHRNN 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 40-197 2.79e-51

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: 165.69  E-value: 2.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  40 EGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVDGGITNGLPI 119
Cdd:cd07220    93 DGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRYVDGGISDNLPQ 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266238920 120 LPFGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAVHFlLKEN 197
Cdd:cd07220   173 YELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRDALRF-LKEN 249
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 40-197 7.81e-41

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: 138.76  E-value: 7.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  40 EGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVDGGITNGLPI 119
Cdd:cd07221    89 DGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDGGVSDNVPF 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266238920 120 LPFGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAVHFlLKEN 197
Cdd:cd07221   169 FDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFRF-LEEN 245
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 33-199 8.99e-38

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: 134.25  E-value: 8.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  33 SCSLQAW--EGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVD 110
Cdd:cd07219    92 SCKMVQMmrQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYID 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920 111 GGITNGLPILPFGRTITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAV 190
Cdd:cd07219   172 GGFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTV 251


                  ....*....
gi 2266238920 191 HFLLKENWF 199
Cdd:cd07219   252 LYLRRLNAV 260
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 46-193 2.40e-31

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: 117.32  E-value: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  46 LPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVDGGITNGLPILPFGRT 125
Cdd:cd07223   104 LPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDGALSNNLPFSDCPST 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2266238920 126 ITISPFSGRLDICPQDKGRVDLYVKFAKQDIMLSLANLVRLNQAMFPPNQEKMESLYQNGFDDAVHFL 193
Cdd:cd07223   184 ITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLDALRFL 251
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 39-130 9.83e-24

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: 92.40  E-value: 9.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  39 WEGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSnFASREDLIKVLLASSFIPVYAGMKPVEYKGEKWVDGGITNGLP 118
Cdd:cd07198    82 RQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGLSNNLP 160

                          90
                  ....*....|..
gi 2266238920 119 ILPFGRTITISP 130
Cdd:cd07198   161 VAELGNTINVSP 172
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 46-189 3.62e-16

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: 73.91  E-value: 3.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  46 LPSNAHE-IAENRLYVSVTNVRNGKNYLF-SNFASREDLIKVLLASSFIPVY-AGMKPVEYKGEKWVDGGITNGLP-ILP 121
Cdd:cd07224    87 LPDDAHErCNRGRIRVAVTQLFPVPRGLLvSSFDSKSDLIDALLASCNIPGYlAPWPATMFRGKLCVDGGFALFIPpTTA 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2266238920 122 FGRTITISPF-SGRLDICPQDKGRVDLYVKFAKQDIMLSLanlvrlnqAMFPPNQEKMESLYQNGFDDA 189
Cdd:cd07224   167 ADRTVRVCPFpASRSSIKGQNLDNDDTEDVPYSRRQLLNW--------ALEPADDAMLLELFNEGYKDA 227
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 23-130 4.30e-13

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: 63.97  E-value: 4.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  23 VSGYLPLGGSscslqawegIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAGMKPV- 101
Cdd:cd01819    42 AATLYPPSSS---------LDNKPRQSLEEALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPa 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2266238920 102 ---------EYKGEKWVDGGITNGLPIL-----PFGRTITISP 130
Cdd:cd01819   113 elytsksnlKEKGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
43-119 2.96e-12

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 63.65  E-value: 2.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2266238920  43 ESILPSNAHEIAEN--RLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYagMKPVEYKGEKWVDGGITNGLPI 119
Cdd:COG4667    95 NELLPFDFETFKASprEFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLL--YPPVEIDGKRYLDGGVADSIPV 171
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 46-119 4.85e-12

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: 63.01  E-value: 4.85e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2266238920  46 LPSNAHEIAEN--RLYVSVTNVRNGKNYLFSNFASREDLIKVLLASSFIPVYAgmKPVEYKGEKWVDGGITNGLPI 119
Cdd:cd07208    92 DPFDFEAFAASpaRFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLF--PPVRIDGEPYVDGGLSDSIPV 165
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 57-193 4.21e-11

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 60.30  E-value: 4.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  57 RLYVSVTNVRNGKNYLFSNFasreDLIKVLLASSFIPvyAGMKPVEYKGEKWVDGGITNGLPILPF---GRTITISpfsg 133
Cdd:COG1752   118 PLAVVATDLETGREVVFDSG----PLADAVRASAAIP--GVFPPVEIDGRLYVDGGVVNNLPVDPAralGADRVIA---- 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2266238920 134 rLDICPQDKGRVDLyVKFAKQDIMLSLANLVRLNQAMFPPNQ--------------EKMESLYQNGFDDAVHFL 193
Cdd:COG1752   188 -VDLNPPLRKLPSL-LDILGRALEIMFNSILRRELALEPADIliepdlsgislldfSRAEELIEAGYEAARRAL 259
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 62-122 9.68e-10

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: 55.69  E-value: 9.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2266238920  62 VTNVRNGKNYLFS-NFASREDLIKVLLASSFIPVYagMKPVEYKGEKWVDGGITNGLPILPF 122
Cdd:pfam01734 130 STALGTRARILLPdDLDDDEDLADAVLASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 58-122 7.60e-08

Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132849 [Multi-domain]  Cd Length: 221  Bit Score: 50.81  E-value: 7.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2266238920  58 LYVSVTNVRNGKNYLFSnfasREDLIKVLLASSFIPVYagMKPVEYKGEKWVDGGITNGLPILPF 122
Cdd:cd07210   104 LAVSVVDLTSRETLLLS----EGDLAEAVAASCAVPPL--FQPVEIGGRPFVDGGVADRLPFDAL 162
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 58-124 8.59e-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: 50.36  E-value: 8.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2266238920  58 LYVSVTNVRNGKNYLFSnfASREDLIKVLLA---SSFIPVYagMKPVEY-KGEKWVDGGITNGLPILPFGR 124
Cdd:cd07207   123 LKVVATDLTTGALVVFS--AETTPDMPVAKAvraSMSIPFV--FKPVRLaKGDVYVDGGVLDNYPVWLFDG 189
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 40-121 2.10e-05

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: 43.30  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2266238920  40 EGIESILPSNAHEIAENRLYVSVTNVRNGKNYLFSnfasREDLIKVLLASSFIPVYagMKPVEYKGEKWVDGGITNGLPI 119
Cdd:cd07205    86 ELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFR----SGSLVRAVRASMSIPGI--FPPVKIDGQLLVDGGVLNNLPV 159


                  ..
gi 2266238920 120 LP 121
Cdd:cd07205   160 DV 161
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 57-119 3.83e-05

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


Pssm-ID: 132866 [Multi-domain]  Cd Length: 175  Bit Score: 42.26  E-value: 3.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2266238920  57 RLYVSVTNVRNGKNYLFSnfasREDLIKVLLASSFIPVYagMKPVEYKGEKWVDGGITNGLPI 119
Cdd:cd07228   103 PFAAVATDLQTGKEVWFR----EGSLIDAIRASISIPGI--FAPVEHNGRLLVDGGVVNPIPV 159
 
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