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Conserved domains on  [gi|742228367|ref|XP_010828199|]
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PREDICTED: patatin-like phospholipase domain-containing protein 4 isoform X1 [Bison bison bison]

Protein Classification

patatin-like phospholipase domain-containing 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

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 ...
 5-250 2.00e-175

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: 482.22  E-value: 2.00e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVASVLLTAPQKIEECNKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07222   81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07222  161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240


                 ....*.
gi 742228367 245 FLVKEN 250
Cdd:cd07222  241 FLKKEN 246
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 5-250 2.00e-175

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: 482.22  E-value: 2.00e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVASVLLTAPQKIEECNKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07222   81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07222  161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240


                 ....*.
gi 742228367 245 FLVKEN 250
Cdd:cd07222  241 FLKKEN 246
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-246 9.65e-18

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 79.95  E-value: 9.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   1 MKHINLSFAACGFLGIYHLGAASALCNHGRnllkDVKACAGASAGSLVASVLLT--APQKIEEcnkftydFAEEIRRQSF 78
Cdd:COG1752    4 RPKIGLVLSGGGARGAAHIGVLKALEEAGI----PPDVIAGTSAGAIVGALYAAgySADELEE-------LWRSLDRRDL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  79 GALTPGYDFM--------------ARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPsredLVKVLLASSF 144
Cdd:COG1752   73 FDLSLPRRLLrldlglspgglldgDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGP----LADAVRASAA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 145 LPIYagLKPVEYKGQRWVDGGFTNSLPVLPV---GRTVTI-SPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLN 220
Cdd:COG1752  149 IPGV--FPPVEIDGRLYVDGGVVNNLPVDPAralGADRVIaVDLNPPLRKLPSLLDILGRALEIMFNSILRRELALEPAD 226

                        250       260       270
                 ....*....|....*....|....*....|...
gi 742228367 221 RALFPP-------SRRTMESLYRRGFDDTSRFL 246
Cdd:COG1752  227 ILIEPDlsgisllDFSRAEELIEAGYEAARRAL 259
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 6-175 5.38e-17

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: 76.49  E-value: 5.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367    6 LSFAACGFLGIYHLGAASALCNHGrnllKDVKACAGASAGSLVASVLLTAPQKIEECNKFTYDFAEEIRRQSFGALTPGY 85
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAG----IRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   86 DFMAR------------LRSGVESILPTNAHELAHGRL------------HVSITNTRTRRNC-LVSSFPSREDLVKVLL 140
Cdd:pfam01734  77 ALLRGligegglfdgdaLRELLRKLLGDLTLEELAARLslllvvalrallTVISTALGTRARIlLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 742228367  141 ASSFLPIYagLKPVEYKGQRWVDGGFTNSLPVLPV 175
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
 
Name Accession Description Interval E-value
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 5-250 2.00e-175

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: 482.22  E-value: 2.00e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVASVLLTAPQKIEECNKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTYKFAEEVRKQRFGAMTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07222   81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07222  161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240


                 ....*.
gi 742228367 245 FLVKEN 250
Cdd:cd07222  241 FLKKEN 246
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 5-248 1.87e-118

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: 338.17  E-value: 1.87e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVASVLLTAPQKIEECnKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07204    1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEAC-SFILKVVSEARRRSLGPLHPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07204   80 FNLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07204  160 GLSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALR 239


                 ....
gi 742228367 245 FLVK 248
Cdd:cd07204  240 FLER 243
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 5-250 7.91e-79

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: 237.63  E-value: 7.91e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVkaCAGASAGSLVASVLLtAPQKIEECNKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07218    2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK--ISGASAGALAACCLL-CDLPLGEMTSDFLRVVREARRHSLGPFSPS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07218   79 FNIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPvGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07218  159 GFSDNLPTLD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALR 237


                 ....*.
gi 742228367 245 FLVKEN 250
Cdd:cd07218  238 FLHRNN 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 5-250 1.80e-72

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: 221.54  E-value: 1.80e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVASVLLTAPQkIEECNKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07220    6 NISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVC-LGECGASVIRVAKEARKRFLGPLHPS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07220   85 FNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVRYVDG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07220  165 GISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRDALR 244


                 ....*.
gi 742228367 245 FLvKEN 250
Cdd:cd07220  245 FL-KEN 249
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 5-246 1.66e-61

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: 193.84  E-value: 1.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSL-VASVLLTAPqkIEECNKFTYDFAEEIRRQSFGALTP 83
Cdd:cd07221    2 SLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALhCVTFLSGLP--LDQILQILMDLVRSARSRNIGILHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  84 GYDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVD 163
Cdd:cd07221   80 SFNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 164 GGFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTS 243
Cdd:cd07221  160 GGVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAF 239


                 ...
gi 742228367 244 RFL 246
Cdd:cd07221  240 RFL 242
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 5-252 1.02e-53

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: 177.78  E-value: 1.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVASVLLTAPQkIEECNKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07219   14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGIS-MDEYLRVLNVGVAEVRKSFLGPLSPS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07219   93 CKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07219  173 GFTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVL 252


                 ....*...
gi 742228367 245 FLVKENWF 252
Cdd:cd07219  253 YLRRLNAV 260
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 6-183 3.66e-52

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


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 167.13  E-value: 3.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   6 LSFAACGFLGIYHLGAASALCNHGRNllkdVKACAGASAGSLVASVLLTAPQKIEECNKFTyDFAEEIRRQSFGALTPGY 85
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLEEALLLLL-RLSREVRLRFDGAFPPTG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  86 DFMARLRSGVESILPTNAHELAHGRLHVSITNtRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDGG 165
Cdd:cd07198   76 RLLGILRQPLLSALPDDAHEDASGKLFISLTR-LTDGENVLVSDTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGG 154

                        170
                 ....*....|....*...
gi 742228367 166 FTNSLPVLPVGRTVTISP 183
Cdd:cd07198  155 LSNNLPVAELGNTINVSP 172
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 5-246 2.50e-44

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: 153.91  E-value: 2.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVAsVLLTAPQKIEECNKFTYDFAEEIRRQSFGALTPG 84
Cdd:cd07223   11 NLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNA-VSIVCGKSADFCCSNLLGMVKHLERLSLGIFHPA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPVEYKGQRWVDG 164
Cdd:cd07223   90 YAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERYIDG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 165 GFTNSLPVLPVGRTVTISPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLNRALFPPSRRTMESLYRRGFDDTSR 244
Cdd:cd07223  170 ALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLDALR 249


                 ..
gi 742228367 245 FL 246
Cdd:cd07223  250 FL 251
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 7-194 1.45e-34

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


Pssm-ID: 132863  Cd Length: 233  Bit Score: 123.99  E-value: 1.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   7 SFAACGFLGIYHLGAASALCNhgRNLLKDVKACAGASAGSLVAsVLLTAPQKIEECNKFTYDFAEEIR----RQSFGALt 82
Cdd:cd07224    3 SFSAAGLLFPYHLGVLSLLIE--AGVINETTPLAGASAGSLAA-ACSASGLSPEEALEATEELAEDCRsngtAFRLGGV- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  83 pgydfmarLRSGVESILPTNAHE-LAHGRLHVSITNTRTR-RNCLVSSFPSREDLVKVLLASSFLPIY-AGLKPVEYKGQ 159
Cdd:cd07224   79 --------LRDELDKTLPDDAHErCNRGRIRVAVTQLFPVpRGLLVSSFDSKSDLIDALLASCNIPGYlAPWPATMFRGK 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 742228367 160 RWVDGGFTNSLP-VLPVGRTVTISPF-SGRLDISPQD 194
Cdd:cd07224  151 LCVDGGFALFIPpTTAADRTVRVCPFpASRSSIKGQN 187
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 6-183 2.47e-30

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: 110.58  E-value: 2.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   6 LSFAACGFLGIYHLGAASALCNHGrnLLKDVKACAGASAGSLVASVLLTapqkieecnkftydfaeeirrqsfgaltPGY 85
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERG--LLDCVTYLAGTSGGAWVAATLYP----------------------------PSS 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  86 DFMARLRSGVEsilptnahELAHGRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAGLKPV----------E 155
Cdd:cd01819   51 SLDNKPRQSLE--------EALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlK 122

                        170       180       190
                 ....*....|....*....|....*....|...
gi 742228367 156 YKGQRWVDGGFTNSLPVL-----PVGRTVTISP 183
Cdd:cd01819  123 EKGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 1-246 9.65e-18

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 79.95  E-value: 9.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   1 MKHINLSFAACGFLGIYHLGAASALCNHGRnllkDVKACAGASAGSLVASVLLT--APQKIEEcnkftydFAEEIRRQSF 78
Cdd:COG1752    4 RPKIGLVLSGGGARGAAHIGVLKALEEAGI----PPDVIAGTSAGAIVGALYAAgySADELEE-------LWRSLDRRDL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  79 GALTPGYDFM--------------ARLRSGVESILPTNAHELAHGRLHVSITNTRTRRNCLVSSFPsredLVKVLLASSF 144
Cdd:COG1752   73 FDLSLPRRLLrldlglspgglldgDPLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFDSGP----LADAVRASAA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367 145 LPIYagLKPVEYKGQRWVDGGFTNSLPVLPV---GRTVTI-SPFSGRLDISPQDKGRLHFYVSITNQEVLLSVANLVRLN 220
Cdd:COG1752  149 IPGV--FPPVEIDGRLYVDGGVVNNLPVDPAralGADRVIaVDLNPPLRKLPSLLDILGRALEIMFNSILRRELALEPAD 226

                        250       260       270
                 ....*....|....*....|....*....|...
gi 742228367 221 RALFPP-------SRRTMESLYRRGFDDTSRFL 246
Cdd:COG1752  227 ILIEPDlsgisllDFSRAEELIEAGYEAARRAL 259
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 6-175 5.38e-17

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: 76.49  E-value: 5.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367    6 LSFAACGFLGIYHLGAASALCNHGrnllKDVKACAGASAGSLVASVLLTAPQKIEECNKFTYDFAEEIRRQSFGALTPGY 85
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAG----IRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   86 DFMAR------------LRSGVESILPTNAHELAHGRL------------HVSITNTRTRRNC-LVSSFPSREDLVKVLL 140
Cdd:pfam01734  77 ALLRGligegglfdgdaLRELLRKLLGDLTLEELAARLslllvvalrallTVISTALGTRARIlLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 742228367  141 ASSFLPIYagLKPVEYKGQRWVDGGFTNSLPVLPV 175
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 4-175 5.04e-13

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


Pssm-ID: 132849 [Multi-domain]  Cd Length: 221  Bit Score: 66.22  E-value: 5.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   4 INLSFAACGFLGIYHLGAASALCNHGrnlLKdVKACAGASAGSLVASvLLTAPQKIEECNKFTY-----DFAEEIRRQSF 78
Cdd:cd07210    1 FALVLSSGFFGFYAHLGFLAALLEMG---LE-PSAISGTSAGALVGG-LFASGISPDEMAELLLslerkDFWMFWDPPLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  79 GALTPGYDFMARLRSgvesILPTNAHELAHGRLHVSITNTRTRRNCLVSSfpsrEDLVKVLLASSFLPIYagLKPVEYKG 158
Cdd:cd07210   76 GGLLSGDRFAALLRE----HLPPDRFEELRIPLAVSVVDLTSRETLLLSE----GDLAEAVAASCAVPPL--FQPVEIGG 145

                        170
                 ....*....|....*..
gi 742228367 159 QRWVDGGFTNSLPVLPV 175
Cdd:cd07210  146 RPFVDGGVADRLPFDAL 162
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 12-172 6.63e-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: 54.92  E-value: 6.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  12 GFLGIYHLGAASALCNHGrnlLKDVKACAGASAGSLVASVLLTAPQK------IEECNKFTY-DFAEEIRRQSfgalTPG 84
Cdd:cd07208    7 GMRGAYTAGVLDAFLEAG---IRPFDLVIGVSAGALNAASYLSGQRGralrinTKYATDPRYlGLRSLLRTGN----LFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  85 YDFMarLRSGVESILPTNAHELAH--GRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAglKPVEYKGQRWV 162
Cdd:cd07208   80 LDFL--YDELPDGLDPFDFEAFAAspARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLF--PPVRIDGEPYV 155

                        170
                 ....*....|
gi 742228367 163 DGGFTNSLPV 172
Cdd:cd07208  156 DGGLSDSIPV 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 8.24e-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: 53.82  E-value: 8.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   5 NLSFAACGFLGIYHLGAASALCNHGrnllKDVKACAGASAGSLVAS-------------VLLTAPQKIEECNKFTYDFaE 71
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKALEEAG----ILKKRVAGTSAGAITAAllalgysaadikdILKETDFAKLLDSPVGLLF-L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  72 EIRRQSFGALTPG---YDFMA-RLRSGVESILPTN----AHELAHGRLHVSITNTRTRRNCLVSSF-PSREDLVKVLLAS 142
Cdd:cd07207   76 LPSLFKEGGLYKGdalEEWLReLLKEKTGNSFATSllrdLDDDLGKDLKVVATDLTTGALVVFSAEtTPDMPVAKAVRAS 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 742228367 143 SFLPIYagLKPVEY-KGQRWVDGGFTNSLPV 172
Cdd:cd07207  156 MSIPFV--FKPVRLaKGDVYVDGGVLDNYPV 184
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 12-174 4.18e-08

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


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 51.39  E-value: 4.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  12 GFLGIYHLGAASALCNHGrnlLKdVKACAGASAGSLVASV--LLTAPQKIEEcnkftydFAEEI--RRQSFGALT-PGYD 86
Cdd:cd07205    9 GARGLAHIGVLKALEEAG---IP-IDIVSGTSAGAIVGALyaAGYSPEEIEE-------RAKLRstDLKALSDLTiPTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  87 FM--ARLRSGVESILPTN------------AHELAHGRLHVSitntrtrrnclvssfpSREDLVKVLLASSFLPIYagLK 152
Cdd:cd07205   78 LLrgDKFLELLDEYFGDRdiedlwipffivATDLTSGKLVVF----------------RSGSLVRAVRASMSIPGI--FP 139

                        170       180
                 ....*....|....*....|..
gi 742228367 153 PVEYKGQRWVDGGFTNSLPVLP 174
Cdd:cd07205  140 PVKIDGQLLVDGGVLNNLPVDV 161
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
109-172 1.56e-06

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


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 48.24  E-value: 1.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742228367 109 GRLHVSITNTRTRRNCLVSSFPSREDLVKVLLASSFLPIYAglKPVEYKGQRWVDGGFTNSLPV 172
Cdd:COG4667  110 REFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLY--PPVEIDGKRYLDGGVADSIPV 171
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 12-171 7.45e-05

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


Pssm-ID: 132845  Cd Length: 298  Bit Score: 42.97  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  12 GFLGIYHLGAASALCNHgrNLLKDVkaCAGASAGSLVASVLLTApqkieecnkfTYdfaEEIrrqsFGALT--PGYDfma 89
Cdd:cd07206   78 ASLGLFHLGVVKALWEQ--DLLPRV--ISGSSAGAIVAALLGTH----------TD---EEL----IGDLTfqEAYE--- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  90 rlRSGVE---SILPTNAHElaHGRLhvsiTNTRTRRNCLVSSfpsredlvkVLLASSFLP-IY----------AGLKPVE 155
Cdd:cd07206  134 --RTGRIiniTVAPAEPHQ--NSRL----LNALTSPNVLIWS---------AVLASCAVPgVFppvmlmaknrDGEIVPY 196

                        170
                 ....*....|....*.
gi 742228367 156 YKGQRWVDGGFTNSLP 171
Cdd:cd07206  197 LPGRKWVDGSVSDDLP 212
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 6-206 2.35e-03

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: 38.59  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   6 LSFAACGFLGIYHLGAASALCNHgrNLLKDVkaCAGASAGSLVASVLLTAPQkiEECNKFtydfaeeiRRQSFGALT--P 83
Cdd:cd07231   71 LLLSGGAALGTFHVGVVRTLVEH--QLLPRV--IAGSSVGSIVCAIIATRTD--EELQSF--------FRALLGDLTfqE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  84 GYDFMARlRSGVeSILPTNAHELAhgRL-------HVSITNTRTRRNCLVSSFPSREDLVKVlLASSFLPIYAGLKPVey 156
Cdd:cd07231  137 AYDRTGR-ILGI-TVCPPRKSEPP--RLlnyltspHVVIWSAVAASCAFPGLFEAQELMAKD-RFGEIVPYHPPGKVS-- 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 742228367 157 KGQRWVDGGFTNSLPVLPVGRTVTISpfsgrldispqdkgrlHFYVSITN 206
Cdd:cd07231  210 SPRRWRDGSLEQDLPMQQLRELFNVN----------------HFIVSQAN 243
Pat17_PNPLA8_PNPLA9_like1 cd07213
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 6-166 3.72e-03

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: 38.04  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367   6 LSFAACGFLGIYHLGAASALCNHGRNLLKDVKACAGASAGSLVASVLLT--APQKIEecnkftyDFAEEIRRQSFGALTP 83
Cdd:cd07213    5 LSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIDLFAGTSAGSLIALGLALgySPRQVL-------KLYEEVGLKVFSKSSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742228367  84 GYD------FMARLRSGVESILPTNAhELAHGRLHVSI----------TNTRTRRNCLVSSFPSRED----LVKVLLASS 143
Cdd:cd07213   78 GGGagnnqyFAAGFLKAFAEVFFGDL-TLGDLKRKVLVpsfqldsgkdDPNRRWKPKLFHNFPGEPDldelLVDVCLRSS 156

                        170       180
                 ....*....|....*....|...
gi 742228367 144 FLPIYagLKPVeykgQRWVDGGF 166
Cdd:cd07213  157 AAPTY--FPSY----QGYVDGGV 173
 
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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