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Conserved domains on  [gi|1622968946|ref|XP_028697631|]
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patatin-like phospholipase domain-containing protein 4 isoform X5 [Macaca mulatta]

Protein Classification

patatin-like phospholipase domain-containing protein; patatin-like phospholipase family protein( domain architecture ID 10163450)

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_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 5-210 4.56e-155

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: 429.44  E-value: 4.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVASVLLTAPEKIEECNQFTYKFAEEIRRQSFGAVTPG 84
Cdd:cd07222     1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  85 YDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDG 164
Cdd:cd07222    81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622968946 165 GLTNALPILPVGRTVTISPFSGRLDISPQDKGQLDLYVNIAKQDIM 210
Cdd:cd07222   161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIM 206
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 5-210 4.56e-155

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: 429.44  E-value: 4.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVASVLLTAPEKIEECNQFTYKFAEEIRRQSFGAVTPG 84
Cdd:cd07222     1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  85 YDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDG 164
Cdd:cd07222    81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622968946 165 GLTNALPILPVGRTVTISPFSGRLDISPQDKGQLDLYVNIAKQDIM 210
Cdd:cd07222   161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIM 206
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 6-175 6.47e-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: 83.43  E-value: 6.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   6 LSFAACGFLGIYHLGAASALcrhgKKLLKDVKAFAGASAGSLVASVLLTAPEKIEECNQFTYKFAEEIRRQSFGAVTPGY 85
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKAL----GEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  86 DIMAQ------------LRSGMESILPPNAHE------------LAQNRLHVSITNTRTRENHLVST-FSSREDLIKVLL 140
Cdd:pfam01734  77 ALLRGligegglfdgdaLRELLRKLLGDLTLEelaarlslllvvALRALLTVISTALGTRARILLPDdLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622968946 141 ASSFVPIYagLKPVEYKGQKWVDGGLTNALPILPV 175
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-175 1.68e-16

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 75.71  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   1 MKHINLSFAACGFLGIYHLGAASALCRHGKKllkdVKAFAGASAGSLVASVLLT--APEKIEEcnqftykFAEEIRRQSF 78
Cdd:COG1752     4 RPKIGLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAgySADELEE-------LWRSLDRRDL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  79 GAVTPGYDIM----AQLRSG----------MESILPPNAHELAQNRLHVSITNTRTRENHLVStfssREDLIKVLLASSF 144
Cdd:COG1752    73 FDLSLPRRLLrldlGLSPGGlldgdplrrlLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAA 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622968946 145 VPIYagLKPVEYKGQKWVDGGLTNALPILPV 175
Cdd:COG1752   149 IPGV--FPPVEIDGRLYVDGGVVNNLPVDPA 177
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 5-210 4.56e-155

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: 429.44  E-value: 4.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVASVLLTAPEKIEECNQFTYKFAEEIRRQSFGAVTPG 84
Cdd:cd07222     1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  85 YDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDG 164
Cdd:cd07222    81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622968946 165 GLTNALPILPVGRTVTISPFSGRLDISPQDKGQLDLYVNIAKQDIM 210
Cdd:cd07222   161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIM 206
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 5-210 1.86e-113

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: 324.30  E-value: 1.86e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVASVLLTAPEKIEECnQFTYKFAEEIRRQSFGAVTPG 84
Cdd:cd07204     1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEAC-SFILKVVSEARRRSLGPLHPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  85 YDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDG 164
Cdd:cd07204    80 FNLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622968946 165 GLTNALPILPVGRTVTISPFSGRLDISPQDKGQLDLYVNIAKQDIM 210
Cdd:cd07204   160 GLSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQ 205
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 5-209 6.17e-67

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: 206.04  E-value: 6.17e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVkaFAGASAGSLVASVLLT-APekIEECNQFTYKFAEEIRRQSFGAVTP 83
Cdd:cd07218     2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK--ISGASAGALAACCLLCdLP--LGEMTSDFLRVVREARRHSLGPFSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  84 GYDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVD 163
Cdd:cd07218    78 SFNIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622968946 164 GGLTNALPILPvGRTVTISPFSGRLDISPQDKGQLDLYVNIAKQDI 209
Cdd:cd07218   158 GGFSDNLPTLD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSI 202
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 5-195 9.13e-62

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: 193.04  E-value: 9.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVASVLLTAPEkIEECNQFTYKFAEEIRRQSFGAVTPG 84
Cdd:cd07220     6 NISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVC-LGECGASVIRVAKEARKRFLGPLHPS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  85 YDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDG 164
Cdd:cd07220    85 FNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRYVDG 164

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622968946 165 GLTNALPILPVGRTVTISPFSGRLDISPQDK 195
Cdd:cd07220   165 GISDNLPQYELKNTITVSPFSGESDICPRDS 195
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 6-183 2.36e-58

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


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 181.77  E-value: 2.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   6 LSFAACGFLGIYHLGAASALCRHGKKllkdVKAFAGASAGSLVASVLLTAPEKIEECNQFTyKFAEEIRRQSFGAVTPGY 85
Cdd:cd07198     1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLL-RLSREVRLRFDGAFPPTG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  86 DIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVStFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDGG 165
Cdd:cd07198    76 RLLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGG 154

                         170
                  ....*....|....*...
gi 1622968946 166 LTNALPILPVGRTVTISP 183
Cdd:cd07198   155 LSNNLPVAELGNTINVSP 172
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 5-206 4.16e-54

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: 173.81  E-value: 4.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSL-VASVLLTAPekIEECNQFTYKFAEEIRRQSFGAVTP 83
Cdd:cd07221     2 SLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALhCVTFLSGLP--LDQILQILMDLVRSARSRNIGILHP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  84 GYDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVD 163
Cdd:cd07221    80 SFNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622968946 164 GGLTNALPILPVGRTVTISPFSGRLDISPQDKGQLDLYVNIAK 206
Cdd:cd07221   160 GGVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTK 202
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 5-194 1.14e-42

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: 147.73  E-value: 1.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVASVLLTAPEkIEECNQFTYKFAEEIRRQSFGAVTPG 84
Cdd:cd07219    14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGIS-MDEYLRVLNVGVAEVRKSFLGPLSPS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  85 YDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDG 164
Cdd:cd07219    93 CKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDG 172

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622968946 165 GLTNALPILPVGRTVTISPFSGRLDISPQD 194
Cdd:cd07219   173 GFTGMQPCSFWTDSITISTFSGQQDICPRD 202
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 5-193 3.48e-40

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: 141.97  E-value: 3.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVAsVLLTAPEKIEECNQFTYKFAEEIRRQSFGAVTPG 84
Cdd:cd07223    11 NLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNA-VSIVCGKSADFCCSNLLGMVKHLERLSLGIFHPA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  85 YDIMAQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPVEYKGQKWVDG 164
Cdd:cd07223    90 YAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDG 169

                         170       180
                  ....*....|....*....|....*....
gi 1622968946 165 GLTNALPILPVGRTVTISPFSGRLDISPQ 193
Cdd:cd07223   170 ALSNNLPFSDCPSTITVSPFHGTVDICPQ 198
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 7-217 9.65e-37

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: 128.61  E-value: 9.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   7 SFAACGFLGIYHLGAASALCRHGkkLLKDVKAFAGASAGSLVASVL---LTApekiEECNQFTYKFAEEIR----RQSFG 79
Cdd:cd07224     3 SFSAAGLLFPYHLGVLSLLIEAG--VINETTPLAGASAGSLAAACSasgLSP----EEALEATEELAEDCRsngtAFRLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  80 AVtpgydimaqLRSGMESILPPNAHELAQN-RLHVSITNTRTR-ENHLVSTFSSREDLIKVLLASSFVPIY-AGLKPVEY 156
Cdd:cd07224    77 GV---------LRDELDKTLPDDAHERCNRgRIRVAVTQLFPVpRGLLVSSFDSKSDLIDALLASCNIPGYlAPWPATMF 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622968946 157 KGQKWVDGGLTNALP-ILPVGRTVTISPF-SGRLDISPQDKGQLDLYVNIAKQDIMSFYSSCP 217
Cdd:cd07224   148 RGKLCVDGGFALFIPpTTAADRTVRVCPFpASRSSIKGQNLDNDDTEDVPYSRRQLLNWALEP 210
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 6-183 5.15e-36

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: 124.06  E-value: 5.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   6 LSFAACGFLGIYHLGAASALCRHGkkLLKDVKAFAGASAGSLVASVLLTapekieecnqftykfaeeirrqsfgavtPGY 85
Cdd:cd01819     1 LSFSGGGFRGMYHAGVLSALAERG--LLDCVTYLAGTSGGAWVAATLYP----------------------------PSS 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  86 DIMAQLRSGMEsilppnahELAQNRLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAGLKPV----------E 155
Cdd:cd01819    51 SLDNKPRQSLE--------EALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlK 122

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622968946 156 YKGQKWVDGGLTNALPIL-----PVGRTVTISP 183
Cdd:cd01819   123 EKGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 6-175 6.47e-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: 83.43  E-value: 6.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   6 LSFAACGFLGIYHLGAASALcrhgKKLLKDVKAFAGASAGSLVASVLLTAPEKIEECNQFTYKFAEEIRRQSFGAVTPGY 85
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKAL----GEAGIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  86 DIMAQ------------LRSGMESILPPNAHE------------LAQNRLHVSITNTRTRENHLVST-FSSREDLIKVLL 140
Cdd:pfam01734  77 ALLRGligegglfdgdaLRELLRKLLGDLTLEelaarlslllvvALRALLTVISTALGTRARILLPDdLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622968946 141 ASSFVPIYagLKPVEYKGQKWVDGGLTNALPILPV 175
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-175 1.68e-16

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 75.71  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   1 MKHINLSFAACGFLGIYHLGAASALCRHGKKllkdVKAFAGASAGSLVASVLLT--APEKIEEcnqftykFAEEIRRQSF 78
Cdd:COG1752     4 RPKIGLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAgySADELEE-------LWRSLDRRDL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  79 GAVTPGYDIM----AQLRSG----------MESILPPNAHELAQNRLHVSITNTRTRENHLVStfssREDLIKVLLASSF 144
Cdd:COG1752    73 FDLSLPRRLLrldlGLSPGGlldgdplrrlLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAA 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622968946 145 VPIYagLKPVEYKGQKWVDGGLTNALPILPV 175
Cdd:COG1752   149 IPGV--FPPVEIDGRLYVDGGVVNNLPVDPA 177
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 4-175 6.79e-14

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: 67.76  E-value: 6.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   4 INLSFAACGFLGIYHLGAASALCRHGKKllkdVKAFAGASAGSLVASvLLTAPEKIEECNQFtykFAEEIRRQSFGAVTP 83
Cdd:cd07210     1 FALVLSSGFFGFYAHLGFLAALLEMGLE----PSAISGTSAGALVGG-LFASGISPDEMAEL---LLSLERKDFWMFWDP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  84 GydimaqLRSG----------MESILPPNAHELAQNRLHVSITNTRTRENHLVStfssREDLIKVLLASSFVPIYagLKP 153
Cdd:cd07210    73 P------LRGGllsgdrfaalLREHLPPDRFEELRIPLAVSVVDLTSRETLLLS----EGDLAEAVAASCAVPPL--FQP 140

                         170       180
                  ....*....|....*....|..
gi 1622968946 154 VEYKGQKWVDGGLTNALPILPV 175
Cdd:cd07210   141 VEIGGRPFVDGGVADRLPFDAL 162
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 12-172 1.77e-09

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: 56.08  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  12 GFLGIYHLGAASALCRHGkklLKDVKAFAGASAGSLVASVLLtapekieeCNQFTY---KFAEEIRRQSFGAV------- 81
Cdd:cd07208     7 GMRGAYTAGVLDAFLEAG---IRPFDLVIGVSAGALNAASYL--------SGQRGRalrINTKYATDPRYLGLrsllrtg 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  82 -TPGYDIMaqLRSGMESILPPNAHELAQN--RLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAglKPVEYKG 158
Cdd:cd07208    76 nLFDLDFL--YDELPDGLDPFDFEAFAASpaRFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLF--PPVRIDG 151

                         170
                  ....*....|....
gi 1622968946 159 QKWVDGGLTNALPI 172
Cdd:cd07208   152 EPYVDGGLSDSIPV 165
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 5-172 2.71e-09

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: 54.59  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   5 NLSFAACGFLGIYHLGAASALCRHGKKllkdVKAFAGASAGSLVASVL---LTAPE---KIEECNQFTYKFAEEIRRQSF 78
Cdd:cd07207     1 NLVFEGGGAKGIAYIGALKALEEAGIL----KKRVAGTSAGAITAALLalgYSAADikdILKETDFAKLLDSPVGLLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  79 GAVTPGYDIM--AQLRSGMESIL----------PPNAHELAQNRLHVSITNTRTRENHLVstFSSREDL--IKVLLA--- 141
Cdd:cd07207    77 PSLFKEGGLYkgDALEEWLRELLkektgnsfatSLLRDLDDDLGKDLKVVATDLTTGALV--VFSAETTpdMPVAKAvra 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622968946 142 SSFVPIYagLKPVEY-KGQKWVDGGLTNALPI 172
Cdd:cd07207   155 SMSIPFV--FKPVRLaKGDVYVDGGVLDNYPV 184
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
96-172 2.31e-08

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 52.86  E-value: 2.31e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622968946  96 ESILPPNAHELAQN--RLHVSITNTRTRENHLVSTFSSREDLIKVLLASSFVPIYAglKPVEYKGQKWVDGGLTNALPI 172
Cdd:COG4667    95 NELLPFDFETFKASprEFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLY--PPVEIDGKRYLDGGVADSIPV 171
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 12-174 1.54e-07

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: 49.47  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  12 GFLGIYHLGAASALCRHGKKllkdVKAFAGASAGSLVASV--LLTAPEKIEEcnqfTYKFAEEIRRQSFGAVTPGYDIM- 88
Cdd:cd07205     9 GARGLAHIGVLKALEEAGIP----IDIVSGTSAGAIVGALyaAGYSPEEIEE----RAKLRSTDLKALSDLTIPTAGLLr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  89 -AQLRSGMESILPPNAHELAQNRLHVSITNTRTRENHLVStfssREDLIKVLLASSFVPIYagLKPVEYKGQKWVDGGLT 167
Cdd:cd07205    81 gDKFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFR----SGSLVRAVRASMSIPGI--FPPVKIDGQLLVDGGVL 154


                  ....*..
gi 1622968946 168 NALPILP 174
Cdd:cd07205   155 NNLPVDV 161
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 6-90 3.99e-05

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: 43.43  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   6 LSFAACGFLGIYHLGAASALCRHGKKLLKDVKAFAGASAGSLVASVLLT--APEKIEecnqftyKFAEEIRRQSFGAVTP 83
Cdd:cd07213     5 LSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIDLFAGTSAGSLIALGLALgySPRQVL-------KLYEEVGLKVFSKSSA 77


                  ....*..
gi 1622968946  84 GYDIMAQ 90
Cdd:cd07213    78 GGGAGNN 84
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 6-176 8.35e-05

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: 42.44  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   6 LSFAACGFLGIYHLGAASALCRHgkKLLKDVkaFAGASAGSLVASVLLTAPEkiEECNQFtykfaeeiRRQSFGAVT--P 83
Cdd:cd07231    71 LLLSGGAALGTFHVGVVRTLVEH--QLLPRV--IAGSSVGSIVCAIIATRTD--EELQSF--------FRALLGDLTfqE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  84 GYDimaqlRSG---MESILPPNAHELAQ--NRL---HVSITNTRTRENHLVSTFSSREDLIKVlLASSFVPIYAGLKPVe 155
Cdd:cd07231   137 AYD-----RTGrilGITVCPPRKSEPPRllNYLtspHVVIWSAVAASCAFPGLFEAQELMAKD-RFGEIVPYHPPGKVS- 209

                         170       180
                  ....*....|....*....|.
gi 1622968946 156 yKGQKWVDGGLTNALPILPVG 176
Cdd:cd07231   210 -SPRRWRDGSLEQDLPMQQLR 229
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 12-172 1.27e-04

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 41.81  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  12 GFLGIYHLGAASALCRHGkkLLKDVkaFAGASAGSLVASVLLTApekieecnqfTYkfaEEIrrqsFGAVT--PGYDima 89
Cdd:cd07206    78 ASLGLFHLGVVKALWEQD--LLPRV--ISGSSAGAIVAALLGTH----------TD---EEL----IGDLTfqEAYE--- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  90 qlRSGME---SILPPNAHElaQNRLhvsiTNTRTRENHLVStfssredliKVLLASSFVP-IY----------AGLKPVE 155
Cdd:cd07206   134 --RTGRIiniTVAPAEPHQ--NSRL----LNALTSPNVLIW---------SAVLASCAVPgVFppvmlmaknrDGEIVPY 196

                         170
                  ....*....|....*..
gi 1622968946 156 YKGQKWVDGGLTNALPI 172
Cdd:cd07206   197 LPGRKWVDGSVSDDLPA 213
Pat_NTE_like_bacteria cd07228
Bacterial patatin-like phospholipase domain containing protein 6; Bacterial patatin-like ...
 4-175 1.29e-04

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: 41.11  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946   4 INLSFAACGFLGIYHLGAASALCRHGKkllkDVKAFAGASAGSLVASVLLTA--PEKIEECNQFTYK-----FAEEIRRQ 76
Cdd:cd07228     1 IGLALGSGGARGWAHIGVLRALEEEGI----EIDIIAGSSIGALVGALYAAGhlDALEEWVRSLSQRdvlrlLDLSASRS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968946  77 SFgavTPGYDIMAQLRSgmesILPPNAHELAQNRLHVSITNTRTREnhlvSTFSSREDLIKVLLASSFVPIYagLKPVEY 156
Cdd:cd07228    77 GL---LKGEKVLEYLRE----IMGGVTIEELPIPFAAVATDLQTGK----EVWFREGSLIDAIRASISIPGI--FAPVEH 143

                         170
                  ....*....|....*....
gi 1622968946 157 KGQKWVDGGLTNALPILPV 175
Cdd:cd07228   144 NGRLLVDGGVVNPIPVSVA 162
 
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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