|
Name |
Accession |
Description |
Interval |
E-value |
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
29-365 |
1.04e-96 |
|
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum cardiophyllum. 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). Patatin-like phospholipase are included in this group. Members of this family have also been found in vertebrates.
Pssm-ID: 132853 [Multi-domain] Cd Length: 349 Bit Score: 293.57 E-value: 1.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 29 GDTISILSIDGGGIKGILPTVVLEDLEQALQIVSNdKNAALADYFDVIAGTSTGGIIATMLAAPNPNDtsRPAFTTPEIL 108
Cdd:cd07214 1 GKFITVLSIDGGGIRGIIPATILEFLEGKLQELDG-PDARIADYFDVIAGTSTGGLITAMLTAPNENK--RPLFAAKDIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 109 EFYLKYGPSIFNQTSAS-GWTEDSPR----PKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFSTFK-KD 182
Cdd:cd07214 78 QFYLENGPKIFPQSTGQfEDDRKKLRsllgPKYDGVYLHDLLNELLGDTRLSDTLTNVVIPTFDIKLLQPVIFSSSKaKN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 183 VPGLDAKLADICIGTSAAPSQLPPYQFLN---GFNI--FNLVDGFVTAANPALVAVSEVIQELNEKNSNFIPVTANKPTK 257
Cdd:cd07214 158 DKLTNARLADVCISTSAAPTYFPAHYFTTedsNGDIreFNLVDGGVAANNPTLLAISEVTKEIIKDNPFFASIKPLDYKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 258 IVLLSIGTGRNGETQGVDANIARFI---SANNWIKVMSAGLAMSAQHMNEYHLKAVFPDLPSSDNYhLRIEEYNLDPSMG 334
Cdd:cd07214 238 LLVLSLGTGSAEESYKYNAAAKWGLitwLSENG*TPIIDIFSNASSDMVDYHLSVIFQALDSEKNY-LRIQDDSLTGTAS 316
|
330 340 350
....*....|....*....|....*....|..
gi 922331704 335 A-DNVTIESMENLIQAGKDLLEQNVKVIDINS 365
Cdd:cd07214 317 SvDDATEENLEKLVEIGKKLLKKPVSRVNLET 348
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
34-354 |
1.02e-65 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 212.07 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALqivsndkNAALADYFDVIAGTSTGGIIATMLAApnpndtsrpAFTTPEILEFYLK 113
Cdd:COG3621 9 ILSLDGGGIRGLIPARILAELEERL-------GKPLAEYFDLIAGTSTGGIIALGLAA---------GYSAEEILDLYEE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFNQTSASGWTE--DSPRPKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFSTFK-KDVPGLDAKL 190
Cdd:COG3621 73 EGKEIFPKSRWRKLLSlrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFKSPHaKFDRDRDFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 191 ADICIGTSAAPSQLPPYQFLNGFN-IFNLVDGFVTAANPALVAVSEVIQELNEKNSNfipvtankptkIVLLSIGTGRNG 269
Cdd:COG3621 153 VDVARATSAAPTYFPPAQIKNLTGeGYALIDGGVFANNPALCALAEALKLLGPDLDD-----------ILVLSLGTGTAP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 270 ETQGVDAniARFISANNWIKVMsAGLAMSAQ-HMNEYHLKAVFPdlpssDNYHlRIEEYnLDPSMGADNVTiESMENLIQ 348
Cdd:COG3621 222 RSIPYKK--VKNWGALGWLLPL-IDILMDAQsDAVDYQLRQLLG-----DRYY-RLDPE-LPEEIALDDNA-ENIEALLA 290
|
....*.
gi 922331704 349 AGKDLL 354
Cdd:COG3621 291 AAEKLI 296
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
34-352 |
1.52e-41 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 149.18 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALqivsndkNAALADYFDVIAGTSTGGIIATMLAAPNPndtsrpaftTPEILEFYLK 113
Cdd:NF041079 3 ILSLSGGGYRGLYTASVLAELEEQF-------GRPIADHFDLICGTSIGGILALALALEIP---------ARELVELFEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFNQ-----TSASGWTedspRPKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFST-----FKKDv 183
Cdd:NF041079 67 HGKDIFPKrkwprRLLGLLK----KPKYSSEPLREVLEEIFGDKTIGDLKHRVLIPAVNYTTGKPQVFKTphhpdFTRD- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 184 pgLDAKLADICIGTSAAPSQLPPYQFLNGfnifNLVDGFVTAANPALVAVSEVIQELNeknsnfipvtaNKPTKIVLLSI 263
Cdd:NF041079 142 --HKLKLVDVALATSAAPTYFPLHEFDNE----QFVDGGLVANNPGLLGLHEALHFLG-----------VPYDDVRILSI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 264 GTGRNGETQGVDANIAR-FISANNWIKVMSagLAMSAQ-HMNEYHLKAVFpdlpsSDNYhLRIEEYNLD---PSMGADNV 338
Cdd:NF041079 205 GTLSSKFTVRPSLKRKRgFLDWGGGKRLFE--LTMSAQeQLVDFMLQHIL-----GDRY-LRIDDVPTNeqaKDLGLDNA 276
|
330
....*....|....
gi 922331704 339 TIESMENLIQAGKD 352
Cdd:NF041079 277 SEAALETLLGRAKQ 290
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
35-233 |
5.36e-18 |
|
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: 81.50 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 35 LSIDGGGIKGILPTVVLEDLEQALqivsndknaalaDYFDVIAGTSTGGIIATMLAAPNPNDTSRPAFttpeiLEFYLKY 114
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAG------------IRFDVISGTSAGAINAALLALGRDPEEIEDLL-----LELDLNL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 115 GPSIFNQTSASGWTEDS----PRPKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFSTFKKDVPGL---- 186
Cdd:pfam01734 64 FLSLIRKRALSLLALLRgligEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARIllpd 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 922331704 187 ----DAKLADICIGTSAAPSQLPPYQFlnGFNIFnlVDGFVTAANPALVAV 233
Cdd:pfam01734 144 dlddDEDLADAVLASSALPGVFPPVRL--DGELY--VDGGLVDNVPVEAAL 190
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
29-365 |
1.04e-96 |
|
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum cardiophyllum. 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). Patatin-like phospholipase are included in this group. Members of this family have also been found in vertebrates.
Pssm-ID: 132853 [Multi-domain] Cd Length: 349 Bit Score: 293.57 E-value: 1.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 29 GDTISILSIDGGGIKGILPTVVLEDLEQALQIVSNdKNAALADYFDVIAGTSTGGIIATMLAAPNPNDtsRPAFTTPEIL 108
Cdd:cd07214 1 GKFITVLSIDGGGIRGIIPATILEFLEGKLQELDG-PDARIADYFDVIAGTSTGGLITAMLTAPNENK--RPLFAAKDIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 109 EFYLKYGPSIFNQTSAS-GWTEDSPR----PKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFSTFK-KD 182
Cdd:cd07214 78 QFYLENGPKIFPQSTGQfEDDRKKLRsllgPKYDGVYLHDLLNELLGDTRLSDTLTNVVIPTFDIKLLQPVIFSSSKaKN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 183 VPGLDAKLADICIGTSAAPSQLPPYQFLN---GFNI--FNLVDGFVTAANPALVAVSEVIQELNEKNSNFIPVTANKPTK 257
Cdd:cd07214 158 DKLTNARLADVCISTSAAPTYFPAHYFTTedsNGDIreFNLVDGGVAANNPTLLAISEVTKEIIKDNPFFASIKPLDYKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 258 IVLLSIGTGRNGETQGVDANIARFI---SANNWIKVMSAGLAMSAQHMNEYHLKAVFPDLPSSDNYhLRIEEYNLDPSMG 334
Cdd:cd07214 238 LLVLSLGTGSAEESYKYNAAAKWGLitwLSENG*TPIIDIFSNASSDMVDYHLSVIFQALDSEKNY-LRIQDDSLTGTAS 316
|
330 340 350
....*....|....*....|....*....|..
gi 922331704 335 A-DNVTIESMENLIQAGKDLLEQNVKVIDINS 365
Cdd:cd07214 317 SvDDATEENLEKLVEIGKKLLKKPVSRVNLET 348
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
34-354 |
1.02e-65 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 212.07 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALqivsndkNAALADYFDVIAGTSTGGIIATMLAApnpndtsrpAFTTPEILEFYLK 113
Cdd:COG3621 9 ILSLDGGGIRGLIPARILAELEERL-------GKPLAEYFDLIAGTSTGGIIALGLAA---------GYSAEEILDLYEE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFNQTSASGWTE--DSPRPKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFSTFK-KDVPGLDAKL 190
Cdd:COG3621 73 EGKEIFPKSRWRKLLSlrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTPVLIPSYDLDNGKPVFFKSPHaKFDRDRDFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 191 ADICIGTSAAPSQLPPYQFLNGFN-IFNLVDGFVTAANPALVAVSEVIQELNEKNSNfipvtankptkIVLLSIGTGRNG 269
Cdd:COG3621 153 VDVARATSAAPTYFPPAQIKNLTGeGYALIDGGVFANNPALCALAEALKLLGPDLDD-----------ILVLSLGTGTAP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 270 ETQGVDAniARFISANNWIKVMsAGLAMSAQ-HMNEYHLKAVFPdlpssDNYHlRIEEYnLDPSMGADNVTiESMENLIQ 348
Cdd:COG3621 222 RSIPYKK--VKNWGALGWLLPL-IDILMDAQsDAVDYQLRQLLG-----DRYY-RLDPE-LPEEIALDDNA-ENIEALLA 290
|
....*.
gi 922331704 349 AGKDLL 354
Cdd:COG3621 291 AAEKLI 296
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
34-355 |
7.66e-61 |
|
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
Pssm-ID: 132838 [Multi-domain] Cd Length: 258 Bit Score: 197.94 E-value: 7.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALQivsndKNAALADYFDVIAGTSTGGIIATMLAAPNpndtsrpaFTTPEILEFYLK 113
Cdd:cd07199 1 ILSLDGGGIRGIIPAEILAELEKRLG-----KPSRIADLFDLIAGTSTGGIIALGLALGR--------YSAEELVELYEE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFnqtsasgwtedsprpkydgiflrdkvgeilqetrlhdtlTNLVITSFDILKLHPIVFSTFK--KDVPGLDAKLA 191
Cdd:cd07199 68 LGRKIF---------------------------------------PRVLVTAYDLSTGKPVVFSNYDaeEPDDDDDFKLW 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 192 DICIGTSAAPSQLPPYQFLNGFNIFNLVDGFVTAANPALVAVSEVIQELNEKNSNfipvtankptkIVLLSIGTGRNGET 271
Cdd:cd07199 109 DVARATSAAPTYFPPAVIESGGDEGAFVDGGVAANNPALLALAEALRLLAPDKDD-----------ILVLSLGTGTSPSS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 272 QGVDANIAR-FISANNWIkvmsAGLAMSAQ-HMNEYHLKAVFPDLPSSDNYhLRIEEYNLDPSMGADNVTIESMENLIQA 349
Cdd:cd07199 178 SSSKKASRWgGLGWGRPL----LDILMDAQsDGVDQWLDLLFGSLDSKDNY-LRINPPLPGPIPALDDASEANLLALDSA 252
|
....*.
gi 922331704 350 GKDLLE 355
Cdd:cd07199 253 AFELIE 258
|
|
| Pat17_PNPLA8_PNPLA9_like2 |
cd07215 |
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ... |
34-362 |
8.32e-60 |
|
Patatin-like phospholipase of bacteria; 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: 132854 [Multi-domain] Cd Length: 329 Bit Score: 197.63 E-value: 8.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALQIVSNDKNAALADYFDVIAGTSTGGIIATMLAApnPNDTSRPAFTTPEILEFYLK 113
Cdd:cd07215 2 ILSIDGGGIRGIIPATILVSVEEKLQKKTGNPEARLADYFDLVAGTSTGGILTCLYLC--PNESGRPKFSAKEALNFYLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFNQTSASGWTEDSP--RPKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFSTFK-KDVPGLDAKL 190
Cdd:cd07215 80 RGNYIFKKKIWNKIKSRGGflNEKYSHKPLEEVLLEYFGDTKLSELLKPCLITSYDIERRSPHFFKSHTaIKNEQRDFYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 191 ADICIGTSAAPSQLPPYQFLNGFNI-FNLVDGFVTAANPALVAVSEVIQELNEKNsnfIPVTANkptKIVLLSIGTGRNg 269
Cdd:cd07215 160 RDVARATSAAPTYFEPARIHSLTGEkYTLIDGGVFANNPTLCAYAEARKLKFEQP---GKPTAK---DMIILSLGTGKN- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 270 eTQGVDANIARFISANNWIKVMSAGLAMSAQHMNEYHLKAVFPDLPSSDNYHlRIEEYNLDPSMGADNVTIESMENLIQA 349
Cdd:cd07215 233 -KKSYTYEKVKDWGLLGWAKPLIDIMMDGASQTVDYQLKQIFDAEGDQQQYL-RIQPELEDADPEMDDASPENLEKLREV 310
|
330
....*....|...
gi 922331704 350 GKDLLEQNVKVID 362
Cdd:cd07215 311 GQALAEDHKDQLD 323
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
34-352 |
1.52e-41 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 149.18 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALqivsndkNAALADYFDVIAGTSTGGIIATMLAAPNPndtsrpaftTPEILEFYLK 113
Cdd:NF041079 3 ILSLSGGGYRGLYTASVLAELEEQF-------GRPIADHFDLICGTSIGGILALALALEIP---------ARELVELFEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFNQ-----TSASGWTedspRPKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFST-----FKKDv 183
Cdd:NF041079 67 HGKDIFPKrkwprRLLGLLK----KPKYSSEPLREVLEEIFGDKTIGDLKHRVLIPAVNYTTGKPQVFKTphhpdFTRD- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 184 pgLDAKLADICIGTSAAPSQLPPYQFLNGfnifNLVDGFVTAANPALVAVSEVIQELNeknsnfipvtaNKPTKIVLLSI 263
Cdd:NF041079 142 --HKLKLVDVALATSAAPTYFPLHEFDNE----QFVDGGLVANNPGLLGLHEALHFLG-----------VPYDDVRILSI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 264 GTGRNGETQGVDANIAR-FISANNWIKVMSagLAMSAQ-HMNEYHLKAVFpdlpsSDNYhLRIEEYNLD---PSMGADNV 338
Cdd:NF041079 205 GTLSSKFTVRPSLKRKRgFLDWGGGKRLFE--LTMSAQeQLVDFMLQHIL-----GDRY-LRIDDVPTNeqaKDLGLDNA 276
|
330
....*....|....
gi 922331704 339 TIESMENLIQAGKD 352
Cdd:NF041079 277 SEAALETLLGRAKQ 290
|
|
| Pat17_PNPLA8_PNPLA9_like1 |
cd07213 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
34-269 |
1.81e-32 |
|
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: 124.32 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALQivsndknaALADYFDVIAGTSTGGIIATMLAApnpndtsrpAFTTPEILEFYLK 113
Cdd:cd07213 4 ILSLDGGGVKGIVQLVLLKRLAEEFP--------SFLDQIDLFAGTSAGSLIALGLAL---------GYSPRQVLKLYEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFNQTSA-SGWTEDSPRPKYDGIFLRDKvgeILQETRLHDTLTNLVITSFDiLKLH---------PIVFSTFKKDv 183
Cdd:cd07213 67 VGLKVFSKSSAgGGAGNNQYFAAGFLKAFAEV---FFGDLTLGDLKRKVLVPSFQ-LDSGkddpnrrwkPKLFHNFPGE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 184 PGLDAKLADICIGTSAAPSQLPPYQflngfnifNLVDGFVTAANPALVAVSEVIqelNEKNSNFipvtanKPTKIVLLSI 263
Cdd:cd07213 142 PDLDELLVDVCLRSSAAPTYFPSYQ--------GYVDGGVFANNPSLCAIAQAI---GEEGLNI------DLKDIVVLSL 204
|
....*.
gi 922331704 264 GTGRNG 269
Cdd:cd07213 205 GTGRPP 210
|
|
| Pat17_PNPLA8_PNPLA9_like3 |
cd07216 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
34-267 |
7.32e-24 |
|
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
Pssm-ID: 132855 [Multi-domain] Cd Length: 309 Bit Score: 100.84 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALQIVSNDKNAAL-ADYFDVIAGTSTGGIIATMLAapnpndtsRPAFTTPEILEFYL 112
Cdd:cd07216 3 LLSLDGGGVRGLSSLLILKEIMERIDPKEGLDEPPKpCDYFDLIGGTSTGGLIAIMLG--------RLRMTVDECIDAYT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 113 KYGPSIFNQTSASGWTEDS-PRPKYDGIFLRDKVGEILQETRLHDTLTNL----------VITSFDILKLHPIVFSTFK- 180
Cdd:cd07216 75 RLAKKIFSRKRLRLIIGDLrTGARFDSKKLAEAIKVILKELGNDEDDLLDegeedgckvfVCATDKDVTGKAVRLRSYPs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 181 KDVPGLDAKLAdICI---GTSAAPSQLPPYQFLNGFNIFnlVDGFVTAANPalvaVSEViqeLNEKNSNFiPVTANKPTk 257
Cdd:cd07216 155 KDEPSLYKNAT-IWEaarATSAAPTFFDPVKIGPGGRTF--VDGGLGANNP----IREV---WSEAVSLW-EGLARLVG- 222
|
250
....*....|
gi 922331704 258 iVLLSIGTGR 267
Cdd:cd07216 223 -CLVSIGTGT 231
|
|
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
34-266 |
1.22e-22 |
|
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: 132856 [Multi-domain] Cd Length: 344 Bit Score: 97.95 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALQIVSNDKNAALADYFDVIAGTSTGGIIATMLAApnpndtsrpAFTTPEILEFYLK 113
Cdd:cd07217 3 ILALDGGGIRGLLSVEILGRIEKDLRTHLDDPEFRLGDYFDFVGGTSTGSIIAACIAL---------GMSVTDLLSFYTL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFNQTsasgWTEDSPRPKYDGIF-----LRDKVGEILQETRLHD----TLTNLVITSFDILKLHPI-------VFS 177
Cdd:cd07217 74 NGVNMFDKA----WLAQRLFLNKLYNQydptnLGKKLNTVFPETTLGDdtlrTLLMIVTRNATTGSPWPVcnnpeakYND 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 178 TFKKDvPGLDAKLADICIGTSAAPSQLPPYQFLNGFNI-FNLVDGFVTA-ANPALVAVSEVIQELNEKNsnfIPVTANkp 255
Cdd:cd07217 150 SDRSD-CNLDLPLWQLVRASTAAPTFFPPEVVSIAPGTaFVFVDGGVTTyNNPAFQAFLMATAKPYKLN---WEVGAD-- 223
|
250
....*....|.
gi 922331704 256 tKIVLLSIGTG 266
Cdd:cd07217 224 -NLLLVSVGTG 233
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
35-233 |
5.36e-18 |
|
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: 81.50 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 35 LSIDGGGIKGILPTVVLEDLEQALqivsndknaalaDYFDVIAGTSTGGIIATMLAAPNPNDTSRPAFttpeiLEFYLKY 114
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAG------------IRFDVISGTSAGAINAALLALGRDPEEIEDLL-----LELDLNL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 115 GPSIFNQTSASGWTEDS----PRPKYDGIFLRDKVGEILQETRLHDTLTNLVITSFDILKLHPIVFSTFKKDVPGL---- 186
Cdd:pfam01734 64 FLSLIRKRALSLLALLRgligEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARIllpd 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 922331704 187 ----DAKLADICIGTSAAPSQLPPYQFlnGFNIFnlVDGFVTAANPALVAV 233
Cdd:pfam01734 144 dlddDEDLADAVLASSALPGVFPPVRL--DGELY--VDGGLVDNVPVEAAL 190
|
|
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
25-235 |
1.13e-15 |
|
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial phospholipase which maintains mitochondrial integrity. PNPLA8 is also known as iPLA2-gamma. In humans, it is predominantly expressed in heart tissue. iPLA2-gamma can catalyze both phospholipase A1 and A2 reactions (PLA1 and PLA2 respectively). This family includes PNPLA8 (iPLA2-gamma) from Homo sapiens and iPLA2-2 from Mus musculus.
Pssm-ID: 132850 [Multi-domain] Cd Length: 308 Bit Score: 77.30 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 25 PPSYGDTISILSIDGGGIKGILPTVVLEDLEQALQivsndknAALADYFDVIAGTSTGGIIATMLAApnpndtsrPAFTT 104
Cdd:cd07211 1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTG-------KPIHELFDYICGVSTGAILAFLLGL--------KKMSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 105 PEILEFYLKYGPSIFNQTSAS------GWTEdsprPKYDGIFLRDKVGEILQETRLHDTLTNL-------VITSFDILKL 171
Cdd:cd07211 66 DECEELYRKLGKDVFSQNTYIsgtsrlVLSH----AYYDTETWEKILKEMMGSDELIDTSADPncpkvacVSTQVNRTPL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922331704 172 HPIVFST--FKKDVP-----GLDAKLADICIGTSAAPSQLPPYQfLNGfNIFNlvDGFVTAANPALVAVSE 235
Cdd:cd07211 142 KPYVFRNynHPPGTRshylgSCKHKLWEAIRASSAAPGYFEEFK-LGN-NLHQ--DGGLLANNPTALALHE 208
|
|
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
34-294 |
3.12e-14 |
|
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent phospholipase that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position. PNPLA9 is also known as PLA2G6 (phospholipase A2 group VI) or iPLA2beta. PLA2G6 is stimulated by ATP and inhibited by bromoenol lactone (BEL). In humans, PNPLA9 in expressed ubiquitously and is involved in signal transduction, cell proliferation, and apoptotic cell death. Mutations in human PLA2G6 leads to infantile neuroaxonal dystrophy (INAD) and idiopathic neurodegeneration with brain iron accumulation (NBIA). This family includes PLA2G6 from Homo sapiens and Rattus norvegicus.
Pssm-ID: 132851 [Multi-domain] Cd Length: 312 Bit Score: 73.13 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 34 ILSIDGGGIKGILPTVVLEDLEQALqivsndkNAALADYFDVIAGTSTGGIIATMLAApnpndtsrpAFTTPEILEFYLK 113
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKAL-------GRPIRELFDWIAGTSTGGILALALLH---------GKSLREARRLYLR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 114 YGPSIFnqtsasgwteDSPRPKYDG---IFLRDKVGEilqETRLHD-TLTNLVITSFDI----LKLH-------PIVFST 178
Cdd:cd07212 65 MKDRVF----------DGSRPYNSEpleEFLKREFGE---DTKMTDvKYPRLMVTGVLAdrqpVQLHlfrnydpPEDVEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 179 FKKDVPGLD-AKLADICI-----GTSAAPSQLPPyqfLNGFnifnlVDGFVTAANPALVAVSEvIQELNEKNSNFipVTA 252
Cdd:cd07212 132 PEKNANFLPpTDPAEQLLwraarSSGAAPTYFRP---MGRF-----LDGGLIANNPTLDAMTE-IHEYNKTLKSK--GRK 200
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 922331704 253 NKPTKI-VLLSIGTGRNGETQGVDANIARFISANNWIKVMSAG 294
Cdd:cd07212 201 NKVKKIgCVVSLGTGIIPQTPVNTVDVFRPSNPWELAKTVFGA 243
|
|
| Patatin_and_cPLA2 |
cd01819 |
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ... |
35-100 |
2.69e-04 |
|
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: 41.25 E-value: 2.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922331704 35 LSIDGGGIKGILPTVVLEDLEqalqivsndkNAALADYFDVIAGTSTGGIIATMLAAPNPNDTSRP 100
Cdd:cd01819 1 LSFSGGGFRGMYHAGVLSALA----------ERGLLDCVTYLAGTSGGAWVAATLYPPSSSLDNKP 56
|
|
| Pat_ExoU_VipD_like |
cd07207 |
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ... |
35-177 |
3.70e-04 |
|
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: 41.50 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922331704 35 LSIDGGGIKGILPTVVLEDLEQAlqivsndknaalaDYFDV-IAGTSTGGIIATMLAAP-NPNDTSRPAFTTPeILEFYL 112
Cdd:cd07207 2 LVFEGGGAKGIAYIGALKALEEA-------------GILKKrVAGTSAGAITAALLALGySAADIKDILKETD-FAKLLD 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922331704 113 KYGPSIFNqtsasGWTEDSPRPKYDGIFLRDKVGEILQETRLHDTLT------------NLVITSFDILKLHPIVFS 177
Cdd:cd07207 68 SPVGLLFL-----LPSLFKEGGLYKGDALEEWLRELLKEKTGNSFATsllrdldddlgkDLKVVATDLTTGALVVFS 139
|
|
| |
