|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
463-707 |
4.51e-149 |
|
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: 437.07 E-value: 4.51e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 463 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 542
Cdd:cd07211 1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 543 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAA----------------------------- 592
Cdd:cd07211 81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACvstqvnrtplkpyvfrnynhppgtrshyl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 593 --------------------------------DGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVTY 639
Cdd:cd07211 161 gsckhklweairassaapgyfeefklgnnlhqDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGGY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767947957 640 TSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 707
Cdd:cd07211 241 TSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
470-704 |
2.59e-37 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 141.58 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 470 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 549
Cdd:COG3621 7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 550 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARN---PT------CPKV------------------------AA--- 592
Cdd:COG3621 86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTPvliPSydldngKPVFfksphakfdrdrdfllvdvaratsAApty 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 593 -----------------DGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVTYTSLKTKLSNVINS 652
Cdd:COG3621 166 fppaqiknltgegyaliDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVKNWGALGWLLPLIDI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767947957 653 ATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 704
Cdd:COG3621 245 LMDaqSDAVDYQLRQLL-GDRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
471-694 |
5.34e-19 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 88.71 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 471 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 549
Cdd:NF041079 2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 550 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTC----------PKV-------------------------AA-- 592
Cdd:NF041079 80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVLipavnyttgkPQVfktphhpdftrdhklklvdvalatsAApt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 593 -------------DGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SLKTKLS------- 647
Cdd:NF041079 159 yfplhefdneqfvDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSLKRKRGfldwggg 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767947957 648 -NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 694
Cdd:NF041079 230 kRLFELTMSAQEqlVDFMLQHIL-GDRYLRID----DVPTNEQAKDLGLD 274
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
473-608 |
2.16e-12 |
|
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: 66.48 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 473 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 546
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767947957 547 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAADGGLLLNNPSALAMHE 608
Cdd:pfam01734 76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRA 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
463-707 |
4.51e-149 |
|
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: 437.07 E-value: 4.51e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 463 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 542
Cdd:cd07211 1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 543 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAA----------------------------- 592
Cdd:cd07211 81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACvstqvnrtplkpyvfrnynhppgtrshyl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 593 --------------------------------DGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVTY 639
Cdd:cd07211 161 gsckhklweairassaapgyfeefklgnnlhqDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGGY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767947957 640 TSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 707
Cdd:cd07211 241 TSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
472-705 |
1.80e-45 |
|
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: 163.27 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 472 ILSIDGGGTRGVVALQTLRKLVELTQKP--VHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFSqNVIVG 549
Cdd:cd07199 1 ILSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP-RVLVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 550 TVKMSWSHAFYDSqTWENILKDRMGSALMIETARN----PTCPK-----------VAADGGLLLNNPSALAMHECKCLWP 614
Cdd:cd07199 80 AYDLSTGKPVVFS-NYDAEEPDDDDDFKLWDVARAtsaaPTYFPpaviesggdegAFVDGGVAANNPALLALAEALRLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 615 -DVPLECIVSLGTGRYESDVRNTVTYT-----SLKTKLSNVINSATDTE--EVHIMLDGLLPPDTYFRFNPVMCENIPLD 686
Cdd:cd07199 159 pDKDDILVLSLGTGTSPSSSSSKKASRwgglgWGRPLLDILMDAQSDGVdqWLDLLFGSLDSKDNYLRINPPLPGPIPAL 238
|
250 260
....*....|....*....|
gi 767947957 687 ESRNEK-LDQLQLEGLKYIE 705
Cdd:cd07199 239 DDASEAnLLALDSAAFELIE 258
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
470-704 |
2.59e-37 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 141.58 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 470 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 549
Cdd:COG3621 7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 550 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARN---PT------CPKV------------------------AA--- 592
Cdd:COG3621 86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTPvliPSydldngKPVFfksphakfdrdrdfllvdvaratsAApty 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 593 -----------------DGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVTYTSLKTKLSNVINS 652
Cdd:COG3621 166 fppaqiknltgegyaliDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVKNWGALGWLLPLIDI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767947957 653 ATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 704
Cdd:COG3621 245 LMDaqSDAVDYQLRQLL-GDRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
|
|
| Pat17_PNPLA8_PNPLA9_like3 |
cd07216 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
470-704 |
3.39e-33 |
|
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: 130.12 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 470 IRILSIDGGGTRGVVALQTLRKLVELTQ---------KPvHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSD 540
Cdd:cd07216 1 LNLLSLDGGGVRGLSSLLILKEIMERIDpkegldeppKP-CDYFDLIGGTSTGGLIAIMLGRLRMTVDECIDAYTRLAKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 541 VFSQ---NVIVGtvkMSWSHAFYDSQTWENIL-------------------------------KDRMGSALMIETARNPT 586
Cdd:cd07216 80 IFSRkrlRLIIG---DLRTGARFDSKKLAEAIkvilkelgndeddlldegeedgckvfvcatdKDVTGKAVRLRSYPSKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 587 CPKV--------------AA-----------------DGGLLLNNPSALAMHECKCLWPDV--PLECIVSLGTG--RYES 631
Cdd:cd07216 157 EPSLyknatiweaaratsAAptffdpvkigpggrtfvDGGLGANNPIREVWSEAVSLWEGLarLVGCLVSIGTGtpSIKS 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767947957 632 DVRNTVtYTSLKTKLsnvINSATDTEEVHIM----LDGLLPPDTYFRFN-PVMCENIPLDEsrNEKLDQLQLEGLKYI 704
Cdd:cd07216 237 LGRSAE-GAGLLKGL---KDLVTDTEAEAKRfsaeHSELDEEGRYFRFNvPHGLEDVGLDE--YEKMEEIVSLTREYL 308
|
|
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
472-707 |
3.86e-22 |
|
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: 97.79 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 472 ILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGLFH-MPLDECEELYRKLGSDVFsqnviVGT 550
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILA--LALLHgKSLREARRLYLRMKDRVF-----DGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 551 VKmswshafYDSQTWENILKDRMGS----------ALMIETA------------RN------------------PTCPKV 590
Cdd:cd07212 74 RP-------YNSEPLEEFLKREFGEdtkmtdvkypRLMVTGVladrqpvqlhlfRNydppedveepeknanflpPTDPAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 591 -----------AA-----------DGGLLLNNPSALAM---HECKCLW-------PDVPLECIVSLGTGRYESDVRNTV- 637
Cdd:cd07212 147 qllwraarssgAAptyfrpmgrflDGGLIANNPTLDAMteiHEYNKTLkskgrknKVKKIGCVVSLGTGIIPQTPVNTVd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 638 ---------TYTSLKT--KLSN-VINSATDTEEVHI--------MLDglLPpdtYFRFNPVMCENIPLDESRNEKLDQLQ 697
Cdd:cd07212 227 vfrpsnpweLAKTVFGakNLGKmVVDQCTASDGAPVdrarawceSIG--IP---YFRFSPPLSKDIMLDETDDEDLVNML 301
|
330
....*....|
gi 767947957 698 LEGLKYIERN 707
Cdd:cd07212 302 WDTEVYIYTH 311
|
|
| Pat17_PNPLA8_PNPLA9_like2 |
cd07215 |
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ... |
471-718 |
3.18e-20 |
|
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: 92.47 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 471 RILSIDGGGTRGVVALQTLR----KLVELTQKPVHQL---FDYICGVSTGAIL-AFML-----GLFHMPLDECEELYRKL 537
Cdd:cd07215 1 RILSIDGGGIRGIIPATILVsveeKLQKKTGNPEARLadyFDLVAGTSTGGILtCLYLcpnesGRPKFSAKEALNFYLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 538 GSDVFSQNvIVGTVKMSW--SHAFYDSQTWENILKDRMGSALMIE-----------------------TARN-------- 584
Cdd:cd07215 81 GNYIFKKK-IWNKIKSRGgfLNEKYSHKPLEEVLLEYFGDTKLSEllkpclitsydierrsphffkshTAIKneqrdfyv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 585 ----------PT------------CPKVAADGGLLLNNPSALAMHECKCLWPDVPlEC-------IVSLGTGryesdvRN 635
Cdd:cd07215 160 rdvaratsaaPTyfeparihsltgEKYTLIDGGVFANNPTLCAYAEARKLKFEQP-GKptakdmiILSLGTG------KN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 636 TVTYTSLKTK-----------LSNVINSATDTEEVHI--MLDGLLPPDTYFRFNPVMCENIP-LDESRNEKLDQLQLEGL 701
Cdd:cd07215 233 KKSYTYEKVKdwgllgwakplIDIMMDGASQTVDYQLkqIFDAEGDQQQYLRIQPELEDADPeMDDASPENLEKLREVGQ 312
|
330
....*....|....*..
gi 767947957 702 KYIERNEQKMKKVAKIL 718
Cdd:cd07215 313 ALAEDHKDQLDEIVDRL 329
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
471-694 |
5.34e-19 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 88.71 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 471 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 549
Cdd:NF041079 2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 550 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTC----------PKV-------------------------AA-- 592
Cdd:NF041079 80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVLipavnyttgkPQVfktphhpdftrdhklklvdvalatsAApt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 593 -------------DGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SLKTKLS------- 647
Cdd:NF041079 159 yfplhefdneqfvDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSLKRKRGfldwggg 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767947957 648 -NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 694
Cdd:NF041079 230 kRLFELTMSAQEqlVDFMLQHIL-GDRYLRID----DVPTNEQAKDLGLD 274
|
|
| Pat17_PNPLA8_PNPLA9_like1 |
cd07213 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
471-697 |
1.08e-13 |
|
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: 72.32 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 471 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLfDYICGVSTGAILAFMLGLFhMPLDECEELYRKLGSDVFSQ------ 544
Cdd:cd07213 3 RILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQI-DLFAGTSAGSLIALGLALG-YSPRQVLKLYEEVGLKVFSKssaggg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 545 ----------------NVIVGTVKMSWSH------AF-YDSQ------TWE-----NILKDRMGSALMIE----TARNPT 586
Cdd:cd07213 81 agnnqyfaagflkafaEVFFGDLTLGDLKrkvlvpSFqLDSGkddpnrRWKpklfhNFPGEPDLDELLVDvclrSSAAPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 587 CPKVA---ADGGLLLNNPSALAM-HECKCLWPDVPLECIV--SLGTGR----YESDVRNT----VTYTSLKTKLSNVINS 652
Cdd:cd07213 161 YFPSYqgyVDGGVFANNPSLCAIaQAIGEEGLNIDLKDIVvlSLGTGRppsyLDGANGYGdwglLQWLPDLLDLFMDAGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767947957 653 ATDTEEVHIMLDgllppDTYFRFNPVMCENIPLDESRN-EKLDQLQ 697
Cdd:cd07213 241 DAADFQCRQLLG-----ERYFRLDPVLPANIDLDDNKQiEELVEIA 281
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
473-608 |
2.16e-12 |
|
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: 66.48 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 473 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 546
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767947957 547 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAADGGLLLNNPSALAMHE 608
Cdd:pfam01734 76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRA 137
|
|
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
471-542 |
5.11e-11 |
|
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: 64.82 E-value: 5.11e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767947957 471 RILSIDGGGTRGVVALQTLRKLVELTQK----PVHQL---FDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVF 542
Cdd:cd07217 2 KILALDGGGIRGLLSVEILGRIEKDLRThlddPEFRLgdyFDFVGGTSTGSIIAACIAL-GMSVTDLLSFYTLNGVNMF 79
|
|
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
477-574 |
1.29e-05 |
|
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];
Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 47.59 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 477 GGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLfHMPLDECEELYRKLG-SDVFSQNVIVGTVKMSW 555
Cdd:COG1752 13 GGGARGAAHIGVLKALEEAGIPP-----DVIAGTSAGAIVGALYAA-GYSADELEELWRSLDrRDLFDLSLPRRLLRLDL 86
|
90 100
....*....|....*....|..
gi 767947957 556 SH---AFYDSQTWENILKDRMG 574
Cdd:COG1752 87 GLspgGLLDGDPLRRLLERLLG 108
|
|
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
467-520 |
4.61e-05 |
|
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: 46.28 E-value: 4.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947957 467 GRGIRILSIDGGGTRGVVA---LQTLR-KLVELTQKPVH--QLFDYICGVSTGAILAFML 520
Cdd:cd07214 1 GKFITVLSIDGGGIRGIIPatiLEFLEgKLQELDGPDARiaDYFDVIAGTSTGGLITAML 60
|
|
| Patatin_and_cPLA2 |
cd01819 |
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ... |
473-517 |
5.34e-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: 5.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 767947957 473 LSIDGGGTRGVVALQTLRKLVELTQkpvHQLFDYICGVSTGAILA 517
Cdd:cd01819 1 LSFSGGGFRGMYHAGVLSALAERGL---LDCVTYLAGTSGGAWVA 42
|
|
| |
