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Conserved domains on  [gi|42571733|ref|NP_973957|]
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Acyl transferase/acyl hydrolase/lysophospholipase superfamily protein [Arabidopsis thaliana]

Protein Classification

Pat_like domain-containing protein( domain architecture ID 10163453)

Pat_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 119-287 1.55e-102

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: 298.87  E-value: 1.55e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 119 GFSFSAAGLLFPYHLGVAQLLIEKGYIKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYDCRRNGTAFRLGAVLR 198
Cdd:cd07224   1 GFSFSAAGLLFPYHLGVLSLLIEAGVINETTPLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNGTAFRLGGVLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 199 ESMERLLPDDIHIRSN-GRIRVAITQVFWRPRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPATMFRNRLCVDGGLTLF 277
Cdd:cd07224  81 DELDKTLPDDAHERCNrGRIRVAVTQLFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLAPWPATMFRGKLCVDGGFALF 160

                       170
                ....*....|.
gi 42571733 278 MPP-TAAAKTV 287
Cdd:cd07224 161 IPPtTAADRTV 171
 
Name Accession Description Interval E-value
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 119-287 1.55e-102

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: 298.87  E-value: 1.55e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 119 GFSFSAAGLLFPYHLGVAQLLIEKGYIKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYDCRRNGTAFRLGAVLR 198
Cdd:cd07224   1 GFSFSAAGLLFPYHLGVLSLLIEAGVINETTPLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNGTAFRLGGVLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 199 ESMERLLPDDIHIRSN-GRIRVAITQVFWRPRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPATMFRNRLCVDGGLTLF 277
Cdd:cd07224  81 DELDKTLPDDAHERCNrGRIRVAVTQLFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLAPWPATMFRGKLCVDGGFALF 160

                       170
                ....*....|.
gi 42571733 278 MPP-TAAAKTV 287
Cdd:cd07224 161 IPPtTAADRTV 171
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 121-283 3.79e-15

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: 72.26  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733   121 SFSAAGLLFPYHLGVAQLLIEKGyiKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYD----------------- 183
Cdd:pfam01734   2 VLSGGGARGAYHLGVLKALGEAG--IRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNlflslirkralsllall 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733   184 -CRRNGTAFRLGAVLRESMERLLPDDIHIRSNGRIR------------VAITQVFWRPRGLLVDQFDSKSDLIDAVFTSS 250
Cdd:pfam01734  80 rGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSlllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLASS 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 42571733   251 FIPGYLAPRPatmFRNRLCVDGGLTLFMPPTAA 283
Cdd:pfam01734 160 ALPGVFPPVR---LDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 131-275 9.10e-10

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 57.99  E-value: 9.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 131 YHLGVAQLLIEKGYiketTP--LAGSSAGAIVCAVITSGATMREALEATKELA----YDCRRNGTAFRL----------- 193
Cdd:COG1752  20 AHIGVLKALEEAGI----PPdvIAGTSAGAIVGALYAAGYSADELEELWRSLDrrdlFDLSLPRRLLRLdlglspgglld 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 194 GAVLRESMERLLP----DDIHIR--------SNGRIRVaitqvfwrprgllvdqFDSkSDLIDAVFTSSFIPGYLaprPA 261
Cdd:COG1752  96 GDPLRRLLERLLGdrdfEDLPIPlavvatdlETGREVV----------------FDS-GPLADAVRASAAIPGVF---PP 155

                       170
                ....*....|....
gi 42571733 262 TMFRNRLCVDGGLT 275
Cdd:COG1752 156 VEIDGRLYVDGGVV 169
 
Name Accession Description Interval E-value
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 119-287 1.55e-102

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: 298.87  E-value: 1.55e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 119 GFSFSAAGLLFPYHLGVAQLLIEKGYIKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYDCRRNGTAFRLGAVLR 198
Cdd:cd07224   1 GFSFSAAGLLFPYHLGVLSLLIEAGVINETTPLAGASAGSLAAACSASGLSPEEALEATEELAEDCRSNGTAFRLGGVLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 199 ESMERLLPDDIHIRSN-GRIRVAITQVFWRPRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPATMFRNRLCVDGGLTLF 277
Cdd:cd07224  81 DELDKTLPDDAHERCNrGRIRVAVTQLFPVPRGLLVSSFDSKSDLIDALLASCNIPGYLAPWPATMFRGKLCVDGGFALF 160

                       170
                ....*....|.
gi 42571733 278 MPP-TAAAKTV 287
Cdd:cd07224 161 IPPtTAADRTV 171
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 119-287 7.16e-65

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: 203.35  E-value: 7.16e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 119 GFSFSAAGLLFPYHLGVAQLLIEKGYIKETT--PLAGSSAGAIVCAVITSGATMREALE--ATKELAYDCRRNGTAFRLG 194
Cdd:cd07204   1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNarRIAGASAGAIVAAVVLCGVSMEEACSfiLKVVSEARRRSLGPLHPSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 195 AV---LRESMERLLPDDIHIRSNGRIRVAITQVFWRpRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPaTMFRNRLCVD 271
Cdd:cd07204  81 NLlkiLRQGLEKILPDDAHELASGRLHISLTRVSDG-ENVLVSEFDSKEELIQALVCSCFIPFYCGLIP-PKFRGVRYID 158

                       170
                ....*....|....*.
gi 42571733 272 GGLTLFMPPTAAAKTV 287
Cdd:cd07204 159 GGLSDNLPILDDENTI 174
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 120-287 1.78e-39

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: 135.93  E-value: 1.78e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 120 FSFSAAGLLFPYHLGVAQLLIEKGYIkeTTPLAGSSAGAIVCAVITSGATMREALEATKELAY--DCRRNGTAFRLGAVL 197
Cdd:cd07198   1 LVLSGGGALGIYHVGVAKALRERGPL--IDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSRevRLRFDGAFPPTGRLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 198 ---RESMERLLPDDIHIRSNGRIRVAITQVFWRPRGLLVdqFDSKSDLIDAVFTSSFIPGYLAPRPAtMFRNRLCVDGGL 274
Cdd:cd07198  79 gilRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS--DTSKGELWSAVRASSSIPGYFGPVPL-SFRGRRYGDGGL 155

                       170
                ....*....|...
gi 42571733 275 TLFMPPTAAAKTV 287
Cdd:cd07198 156 SNNLPVAELGNTI 168
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 121-279 1.07e-28

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: 109.73  E-value: 1.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 121 SFSAAGLLFPYHLGVAQLLIE--KGYIKETTPLAGSSAGAIVCAVITsgaTMREALEATKELAYDCRRNGTAFRLGAV-- 196
Cdd:cd07222   3 SFAACGFLGIYHLGAAKALLRhgKKLLKRVKRFAGASAGSLVAAVLL---TAPEKIEECKEFTYKFAEEVRKQRFGAMtp 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 197 -------LRESMERLLPDDIHIRSNGRIRVAITQVFWRpRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPaTMFRNRLC 269
Cdd:cd07222  80 gydfmarLRKGIESILPTDAHELANDRLHVSITNLKTR-KNYLVSNFTSREDLIKVLLASCYVPVYAGLKP-VEYKGQKW 157

                       170
                ....*....|
gi 42571733 270 VDGGLTLFMP 279
Cdd:cd07222 158 IDGGFTNSLP 167
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 121-279 5.31e-26

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: 102.90  E-value: 5.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 121 SFSAAGLLFPYHLGVAQLLIEKG--YIKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYDCRRNG-----TAFRL 193
Cdd:cd07220   8 SFAGCGFLGVYHVGVASCLLEHApfLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFlgplhPSFNL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 194 GAVLRESMERLLPDDIHIRSNGRIRVAITQVfwrPRG--LLVDQFDSKSDLIDAVFTSSFIPGYLAPRPATmFRNRLCVD 271
Cdd:cd07220  88 VKILRDGLLRTLPENAHELASGRLGISLTRV---SDGenVLVSDFNSKEELIQALVCSCFIPVYCGLIPPT-LRGVRYVD 163


                ....*...
gi 42571733 272 GGLTLFMP 279
Cdd:cd07220 164 GGISDNLP 171
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 120-287 1.91e-22

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: 93.30  E-value: 1.91e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 120 FSFSAAGLLFPYHLGVAQLLIEKG--YIKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYDCR-RN-GT---AFR 192
Cdd:cd07221   3 LSFAGCGFLGFYHVGVTRCLSERAphLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARsRNiGIlhpSFN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 193 LGAVLRESMERLLPDDIHIRSNGRIRVAITQVFwRPRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPATmFRNRLCVDG 272
Cdd:cd07221  83 LSKHLRDGLQRHLPDNVHQLISGKMCISLTRVS-DGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPS-FRGVRYVDG 160

                       170
                ....*....|....*
gi 42571733 273 GLTLFMPPTAAAKTV 287
Cdd:cd07221 161 GVSDNVPFFDAKTTI 175
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 121-275 1.25e-21

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: 90.87  E-value: 1.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 121 SFSAAGLLFPYHLGVA--------QLLIEKgyikettpLAGSSAGAIVCAVITSGATMREALEATKELAYDCRRN----- 187
Cdd:cd07218   4 SFAGCGFLGIYHVGVAvclkkyapHLLLNK--------ISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHslgpf 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 188 GTAFRLGAVLRESMERLLPDDIHIRSNGRIRVAITQVfWRPRGLLVDQFDSKSDLIDAVFTSSFIP---GYLAPRpatmF 264
Cdd:cd07218  76 SPSFNIQTCLLEGLQKFLPDDAHERVSGRLHISLTRV-SDGKNVIVSEFESREELLQALLCSCFIPvfsGLLPPK----F 150

                       170
                ....*....|.
gi 42571733 265 RNRLCVDGGLT 275
Cdd:cd07218 151 RGVRYMDGGFS 161
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 107-279 2.15e-17

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: 81.09  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 107 EAEKERRVITSPGFSFSAAGLLFPYHLGVAQLLIEKG--YIKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYDC 184
Cdd:cd07219   2 EQVFKGDPDTPHSISFSGSGFLSFYQAGVVDALRDLAprMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 185 RRN-----GTAFRLGAVLRESMERLLPDDIHIRSNGRIRVAITQVFwRPRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPR 259
Cdd:cd07219  82 RKSflgplSPSCKMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVT-DGENVVVSEFTSKEELIEALYCSCFVPVYCGLI 160

                       170       180
                ....*....|....*....|
gi 42571733 260 PATmFRNRLCVDGGLTLFMP 279
Cdd:cd07219 161 PPT-YRGVRYIDGGFTGMQP 179
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 121-283 3.79e-15

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: 72.26  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733   121 SFSAAGLLFPYHLGVAQLLIEKGyiKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYD----------------- 183
Cdd:pfam01734   2 VLSGGGARGAYHLGVLKALGEAG--IRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNlflslirkralsllall 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733   184 -CRRNGTAFRLGAVLRESMERLLPDDIHIRSNGRIR------------VAITQVFWRPRGLLVDQFDSKSDLIDAVFTSS 250
Cdd:pfam01734  80 rGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSlllvvalralltVISTALGTRARILLPDDLDDDEDLADAVLASS 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 42571733   251 FIPGYLAPRPatmFRNRLCVDGGLTLFMPPTAA 283
Cdd:pfam01734 160 ALPGVFPPVR---LDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 131-275 9.10e-10

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 57.99  E-value: 9.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 131 YHLGVAQLLIEKGYiketTP--LAGSSAGAIVCAVITSGATMREALEATKELA----YDCRRNGTAFRL----------- 193
Cdd:COG1752  20 AHIGVLKALEEAGI----PPdvIAGTSAGAIVGALYAAGYSADELEELWRSLDrrdlFDLSLPRRLLRLdlglspgglld 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 194 GAVLRESMERLLP----DDIHIR--------SNGRIRVaitqvfwrprgllvdqFDSkSDLIDAVFTSSFIPGYLaprPA 261
Cdd:COG1752  96 GDPLRRLLERLLGdrdfEDLPIPlavvatdlETGREVV----------------FDS-GPLADAVRASAAIPGVF---PP 155

                       170
                ....*....|....
gi 42571733 262 TMFRNRLCVDGGLT 275
Cdd:COG1752 156 VEIDGRLYVDGGVV 169
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 120-287 1.83e-08

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: 54.92  E-value: 1.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 120 FSFSAAGLLFPYHLGVAQLLIEKG--YIKETTPLAGSSAGAIVCAVITSGATMREALEATKELAYDCRRNG-----TAFR 192
Cdd:cd07223  12 LSFSGAGYLGLYHVGVTECLRQRAprLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSlgifhPAYA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 193 LGAVLRESMERLLPDDIHIRSNGRIRVAITQvfWRP-RGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPATmFRNRLCVD 271
Cdd:cd07223  92 PIEHIRQQLQESLPPNIHILASQRLGISMTR--WPDgRNFIVTDFATRDELIQALICTLYFPFYCGIIPPE-FRGERYID 168

                       170
                ....*....|....*.
gi 42571733 272 GGLTLFMPPTAAAKTV 287
Cdd:cd07223 169 GALSNNLPFSDCPSTI 184
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 121-280 7.04e-08

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: 50.88  E-value: 7.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 121 SFSAAGLLFPYHLGVAQLLIEKGYIKETTPLAGSSAGAIVCAVITSGATMrealeatkelaydcrrngtafrLGAVLRES 200
Cdd:cd01819   2 SFSGGGFRGMYHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLYPPSSS----------------------LDNKPRQS 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 201 MERLLPDDIHIrsngrirvaITQVFWRPRGLLVDQFDSKSDLIDAVFTSSFIPGYLAPRPATMF--------RNRLC-VD 271
Cdd:cd01819  60 LEEALSGKLWV---------SFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPAELytsksnlkEKGVRlVD 130


                ....*....
gi 42571733 272 GGLTLFMPP 280
Cdd:cd01819 131 GGVSNNLPA 139
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 122-274 1.23e-07

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: 51.19  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 122 FSAAGLLFPYHLGVAQLLIEKGYikETTPLAGSSAGAIVCAVITSGATMRE------ALEATKELAYDCRRNGT-AFRLG 194
Cdd:cd07210   5 LSSGFFGFYAHLGFLAALLEMGL--EPSAISGTSAGALVGGLFASGISPDEmaelllSLERKDFWMFWDPPLRGgLLSGD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 195 AVLRESMERLLPDDIhirSNGRIRVAITQVFWRPRGLlvdQFDSKSDLIDAVFTSSFIPGYLAPRPatmFRNRLCVDGGL 274
Cdd:cd07210  83 RFAALLREHLPPDRF---EELRIPLAVSVVDLTSRET---LLLSEGDLAEAVAASCAVPPLFQPVE---IGGRPFVDGGV 153
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 122-177 2.15e-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: 44.89  E-value: 2.15e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571733 122 FSAAGLLFPYHLGVAQLLIEKGYIkettP--LAGSSAGAIVCAV--------ITSGATMREALEAT 177
Cdd:cd07206  74 LSGGASLGLFHLGVVKALWEQDLL----PrvISGSSAGAIVAALlgthtdeeLIGDLTFQEAYERT 135
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 131-275 4.03e-05

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


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 43.30  E-value: 4.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 131 YHLGVAQLLIEKGyIKettP--LAGSSAGAIVCAVITSGATMREALEATKEL------AYDCRRNGTAFRLGAVLRESME 202
Cdd:cd07205  14 AHIGVLKALEEAG-IP---IdiVSGTSAGAIVGALYAAGYSPEEIEERAKLRstdlkaLSDLTIPTAGLLRGDKFLELLD 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 203 RLLPdDIHIrSNGRIRVAIT---------QVFWRprgllvdqfdskSDLIDAVFTSSFIPGYLAPrpaTMFRNRLCVDGG 273
Cdd:cd07205  90 EYFG-DRDI-EDLWIPFFIVatdltsgklVVFRS------------GSLVRAVRASMSIPGIFPP---VKIDGQLLVDGG 152


                ..
gi 42571733 274 LT 275
Cdd:cd07205 153 VL 154
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 122-274 4.93e-05

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: 43.04  E-value: 4.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 122 FSAAGLLFPYHLGVAQLLIEKGYIKETtpLAGSSAGAIVCAVITSGAT---MREALEAT---KELAYDCRRNGTAFRL-- 193
Cdd:cd07207   4 FEGGGAKGIAYIGALKALEEAGILKKR--VAGTSAGAITAALLALGYSaadIKDILKETdfaKLLDSPVGLLFLLPSLfk 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 194 ------GAVLRESMERLLpddihiRSNGRIRVA--ITQVFWRPRG--LLV---DQFDSKSDLI-----------DAVFTS 249
Cdd:cd07207  82 egglykGDALEEWLRELL------KEKTGNSFAtsLLRDLDDDLGkdLKVvatDLTTGALVVFsaettpdmpvaKAVRAS 155

                       170       180
                ....*....|....*....|....*
gi 42571733 250 SFIPGYLAPRpaTMFRNRLCVDGGL 274
Cdd:cd07207 156 MSIPFVFKPV--RLAKGDVYVDGGV 178
Pat_SDP1-like cd07231
Sugar-Dependent 1 like lipase; Sugar-Dependent 1 (SDP1) lipase has a patatin-like ...
 122-166 2.05e-04

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


Pssm-ID: 132869  Cd Length: 323  Bit Score: 42.05  E-value: 2.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 42571733 122 FSAAGLLFPYHLGVAQLLIEKGYIKETtpLAGSSAGAIVCAVITS 166
Cdd:cd07231  73 LSGGAALGTFHVGVVRTLVEHQLLPRV--IAGSSVGSIVCAIIAT 115
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 131-279 7.64e-04

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 39.97  E-value: 7.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571733 131 YHLGVAQLLIEKGYiketTP--LAGSSAGAIVCAVITSGATMR-EALEAT-KELAYDcrrngTAFRLGAVLRESMERLLP 206
Cdd:cd07209  12 YQAGVLKALAEAGI----EPdiISGTSIGAINGALIAGGDPEAvERLEKLwRELSRE-----DVFLRGLLDRALDFDTLR 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571733 207 dDIHIRSNGRIRVAITQVfwrpRGLLVdQFDSKSD--LIDAVFTSSFIPGYLaprPATMFRNRLCVDGGLTLFMP 279
Cdd:cd07209  83 -LLAILFAGLVIVAVNVL----TGEPV-YFDDIPDgiLPEHLLASAALPPFF---PPVEIDGRYYWDGGVVDNTP 148
 
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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