|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
435-679 |
1.95e-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: 1.95e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 435 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 514
Cdd:cd07211 1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 515 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAA----------------------------- 564
Cdd:cd07211 81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACvstqvnrtplkpyvfrnynhppgtrshyl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 565 --------------------------------DGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVTY 611
Cdd:cd07211 161 gsckhklweairassaapgyfeefklgnnlhqDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGGY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530386008 612 TSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 679
Cdd:cd07211 241 TSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
442-676 |
2.28e-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: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 442 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:COG3621 7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 522 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARN---PT------CPKV------------------------AA--- 564
Cdd:COG3621 86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTPvliPSydldngKPVFfksphakfdrdrdfllvdvaratsAApty 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 565 -----------------DGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVTYTSLKTKLSNVINS 624
Cdd:COG3621 166 fppaqiknltgegyaliDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVKNWGALGWLLPLIDI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 530386008 625 ATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 676
Cdd:COG3621 245 LMDaqSDAVDYQLRQLL-GDRYYRLDPELPEEIALDDN-AENIEALLAAAEKLI 296
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
443-666 |
5.05e-19 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 88.71 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 443 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:NF041079 2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 522 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTC----------PKV-------------------------AA-- 564
Cdd:NF041079 80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVLipavnyttgkPQVfktphhpdftrdhklklvdvalatsAApt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 565 -------------DGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SLKTKLS------- 619
Cdd:NF041079 159 yfplhefdneqfvDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSLKRKRGfldwggg 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530386008 620 -NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 666
Cdd:NF041079 230 kRLFELTMSAQEqlVDFMLQHIL-GDRYLRID----DVPTNEQAKDLGLD 274
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
445-580 |
2.07e-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: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 445 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 518
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530386008 519 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAADGGLLLNNPSALAMHE 580
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 ... |
435-679 |
1.95e-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: 1.95e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 435 DPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVF 514
Cdd:cd07211 1 PPVKGRGIRILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 515 SQNV-IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAA----------------------------- 564
Cdd:cd07211 81 SQNTyISGTSRLVLSHAYYDTETWEKILKEMMGSDELIDTSADPNCPKVACvstqvnrtplkpyvfrnynhppgtrshyl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 565 --------------------------------DGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVR-NTVTY 611
Cdd:cd07211 161 gsckhklweairassaapgyfeefklgnnlhqDGGLLANNPTALALHEAKLLWPDTPIQCLVSVGTGRYPSSVRlETGGY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530386008 612 TSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERN 679
Cdd:cd07211 241 TSLKTKLLNLIDSATDTERVHTALDDLLPPDVYFRFNPVMSECVELDETRPEKLDQLQDDTLEYIKRN 308
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
444-677 |
1.46e-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: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 444 ILSIDGGGTRGVVALQTLRKLVELTQKP--VHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFSqNVIVG 521
Cdd:cd07199 1 ILSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIFP-RVLVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 522 TVKMSWSHAFYDSqTWENILKDRMGSALMIETARN----PTCPK-----------VAADGGLLLNNPSALAMHECKCLWP 586
Cdd:cd07199 80 AYDLSTGKPVVFS-NYDAEEPDDDDDFKLWDVARAtsaaPTYFPpaviesggdegAFVDGGVAANNPALLALAEALRLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 587 -DVPLECIVSLGTGRYESDVRNTVTYT-----SLKTKLSNVINSATDTE--EVHIMLDGLLPPDTYFRFNPVMCENIPLD 658
Cdd:cd07199 159 pDKDDILVLSLGTGTSPSSSSSKKASRwgglgWGRPLLDILMDAQSDGVdqWLDLLFGSLDSKDNYLRINPPLPGPIPAL 238
|
250 260
....*....|....*....|
gi 530386008 659 ESRNEK-LDQLQLEGLKYIE 677
Cdd:cd07199 239 DDASEAnLLALDSAAFELIE 258
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
442-676 |
2.28e-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: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 442 IRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:COG3621 7 FRILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 522 TVKM-SWSHAFYDSQTWENILKDRMGSALMIETARN---PT------CPKV------------------------AA--- 564
Cdd:COG3621 86 LLSLrGLFGPKYDSEGLEKVLKEYFGDTTLGDLKTPvliPSydldngKPVFfksphakfdrdrdfllvdvaratsAApty 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 565 -----------------DGGLLLNNPSALAMHECKCLWpDVPLE--CIVSLGTGRYESDVR-NTVTYTSLKTKLSNVINS 624
Cdd:COG3621 166 fppaqiknltgegyaliDGGVFANNPALCALAEALKLL-GPDLDdiLVLSLGTGTAPRSIPyKKVKNWGALGWLLPLIDI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 530386008 625 ATD--TEEVHIMLDGLLpPDTYFRFNPVMCENIPLDESrNEKLDQLQLEGLKYI 676
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 ... |
442-676 |
3.09e-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: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 442 IRILSIDGGGTRGVVALQTLRKLVELTQ---------KPvHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSD 512
Cdd:cd07216 1 LNLLSLDGGGVRGLSSLLILKEIMERIDpkegldeppKP-CDYFDLIGGTSTGGLIAIMLGRLRMTVDECIDAYTRLAKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 513 VFSQ---NVIVGtvkMSWSHAFYDSQTWENIL-------------------------------KDRMGSALMIETARNPT 558
Cdd:cd07216 80 IFSRkrlRLIIG---DLRTGARFDSKKLAEAIkvilkelgndeddlldegeedgckvfvcatdKDVTGKAVRLRSYPSKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 559 CPKV--------------AA-----------------DGGLLLNNPSALAMHECKCLWPDV--PLECIVSLGTG--RYES 603
Cdd:cd07216 157 EPSLyknatiweaaratsAAptffdpvkigpggrtfvDGGLGANNPIREVWSEAVSLWEGLarLVGCLVSIGTGtpSIKS 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530386008 604 DVRNTVtYTSLKTKLsnvINSATDTEEVHIM----LDGLLPPDTYFRFN-PVMCENIPLDEsrNEKLDQLQLEGLKYI 676
Cdd:cd07216 237 LGRSAE-GAGLLKGL---KDLVTDTEAEAKRfsaeHSELDEEGRYFRFNvPHGLEDVGLDE--YEKMEEIVSLTREYL 308
|
|
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
444-679 |
3.65e-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: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 444 ILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGLFH-MPLDECEELYRKLGSDVFsqnviVGT 522
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILA--LALLHgKSLREARRLYLRMKDRVF-----DGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 523 VKmswshafYDSQTWENILKDRMGS----------ALMIETA------------RN------------------PTCPKV 562
Cdd:cd07212 74 RP-------YNSEPLEEFLKREFGEdtkmtdvkypRLMVTGVladrqpvqlhlfRNydppedveepeknanflpPTDPAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 563 -----------AA-----------DGGLLLNNPSALAM---HECKCLW-------PDVPLECIVSLGTGRYESDVRNTV- 609
Cdd:cd07212 147 qllwraarssgAAptyfrpmgrflDGGLIANNPTLDAMteiHEYNKTLkskgrknKVKKIGCVVSLGTGIIPQTPVNTVd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 610 ---------TYTSLKT--KLSN-VINSATDTEEVHI--------MLDglLPpdtYFRFNPVMCENIPLDESRNEKLDQLQ 669
Cdd:cd07212 227 vfrpsnpweLAKTVFGakNLGKmVVDQCTASDGAPVdrarawceSIG--IP---YFRFSPPLSKDIMLDETDDEDLVNML 301
|
330
....*....|
gi 530386008 670 LEGLKYIERN 679
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 ... |
443-690 |
6.40e-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: 91.70 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 443 RILSIDGGGTRGVVALQTLR----KLVELTQKPVHQL---FDYICGVSTGAIL-AFML-----GLFHMPLDECEELYRKL 509
Cdd:cd07215 1 RILSIDGGGIRGIIPATILVsveeKLQKKTGNPEARLadyFDLVAGTSTGGILtCLYLcpnesGRPKFSAKEALNFYLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 510 GSDVFSQNvIVGTVKMSW--SHAFYDSQTWENILKDRMGSALMIE-----------------------TARN-------- 556
Cdd:cd07215 81 GNYIFKKK-IWNKIKSRGgfLNEKYSHKPLEEVLLEYFGDTKLSEllkpclitsydierrsphffkshTAIKneqrdfyv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 557 ----------PT------------CPKVAADGGLLLNNPSALAMHECKCLWPDVPlEC-------IVSLGTGryesdvRN 607
Cdd:cd07215 160 rdvaratsaaPTyfeparihsltgEKYTLIDGGVFANNPTLCAYAEARKLKFEQP-GKptakdmiILSLGTG------KN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 608 TVTYTSLKTK-----------LSNVINSATDTEEVHI--MLDGLLPPDTYFRFNPVMCENIP-LDESRNEKLDQLQLEGL 673
Cdd:cd07215 233 KKSYTYEKVKdwgllgwakplIDIMMDGASQTVDYQLkqIFDAEGDQQQYLRIQPELEDADPeMDDASPENLEKLREVGQ 312
|
330
....*....|....*..
gi 530386008 674 KYIERNEQKMKKVAKIL 690
Cdd:cd07215 313 ALAEDHKDQLDEIVDRL 329
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
443-666 |
5.05e-19 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 88.71 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 443 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAfmLGL-FHMPLDECEELYRKLGSDVFSQNVIVG 521
Cdd:NF041079 2 QILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILA--LALaLEIPARELVELFEEHGKDIFPKRKWPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 522 TVKMSWSHAFYDSQTWENILKDRMGSALmIETARNPTC----------PKV-------------------------AA-- 564
Cdd:NF041079 80 RLLGLLKKPKYSSEPLREVLEEIFGDKT-IGDLKHRVLipavnyttgkPQVfktphhpdftrdhklklvdvalatsAApt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 565 -------------DGGLLLNNPSALAMHECKCLwPDVPLE--CIVSLGTGryesdvrnTVTYT---SLKTKLS------- 619
Cdd:NF041079 159 yfplhefdneqfvDGGLVANNPGLLGLHEALHF-LGVPYDdvRILSIGTL--------SSKFTvrpSLKRKRGfldwggg 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530386008 620 -NVINSATDTEE--VHIMLDGLLpPDTYFRFNpvmcENIPLDESRNEKLD 666
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 ... |
443-669 |
1.03e-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: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 443 RILSIDGGGTRGVVALQTLRKLVELTQKPVHQLfDYICGVSTGAILAFMLGLFhMPLDECEELYRKLGSDVFSQ------ 516
Cdd:cd07213 3 RILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQI-DLFAGTSAGSLIALGLALG-YSPRQVLKLYEEVGLKVFSKssaggg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 517 ----------------NVIVGTVKMSWSH------AF-YDSQ------TWE-----NILKDRMGSALMIE----TARNPT 558
Cdd:cd07213 81 agnnqyfaagflkafaEVFFGDLTLGDLKrkvlvpSFqLDSGkddpnrRWKpklfhNFPGEPDLDELLVDvclrSSAAPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 559 CPKVA---ADGGLLLNNPSALAM-HECKCLWPDVPLECIV--SLGTGR----YESDVRNT----VTYTSLKTKLSNVINS 624
Cdd:cd07213 161 YFPSYqgyVDGGVFANNPSLCAIaQAIGEEGLNIDLKDIVvlSLGTGRppsyLDGANGYGdwglLQWLPDLLDLFMDAGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 530386008 625 ATDTEEVHIMLDgllppDTYFRFNPVMCENIPLDESRN-EKLDQLQ 669
Cdd:cd07213 241 DAADFQCRQLLG-----ERYFRLDPVLPANIDLDDNKQiEELVEIA 281
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
445-580 |
2.07e-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: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 445 LSIDGGGTRGVVALQTLRKLVELTQKpvhqlFDYICGVSTGAILAFMLGLFHMP---LDECEELYRKLGSDVFS---QNV 518
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIR-----FDVISGTSAGAINAALLALGRDPeeiEDLLLELDLNLFLSLIRkraLSL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530386008 519 IVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAADGGLLLNNPSALAMHE 580
Cdd:pfam01734 76 LALLRGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRA 137
|
|
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
443-514 |
4.85e-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: 4.85e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530386008 443 RILSIDGGGTRGVVALQTLRKLVELTQK----PVHQL---FDYICGVSTGAILAFMLGLfHMPLDECEELYRKLGSDVF 514
Cdd:cd07217 2 KILALDGGGIRGLLSVEILGRIEKDLRThlddPEFRLgdyFDFVGGTSTGSIIAACIAL-GMSVTDLLSFYTLNGVNMF 79
|
|
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
449-546 |
1.23e-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: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 449 GGGTRGVVALQTLRKLVELTQKPvhqlfDYICGVSTGAILAFMLGLfHMPLDECEELYRKLG-SDVFSQNVIVGTVKMSW 527
Cdd:COG1752 13 GGGARGAAHIGVLKALEEAGIPP-----DVIAGTSAGAIVGALYAA-GYSADELEELWRSLDrRDLFDLSLPRRLLRLDL 86
|
90 100
....*....|....*....|..
gi 530386008 528 SH---AFYDSQTWENILKDRMG 546
Cdd:COG1752 87 GLspgGLLDGDPLRRLLERLLG 108
|
|
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
439-492 |
4.39e-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: 4.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386008 439 GRGIRILSIDGGGTRGVVA---LQTLR-KLVELTQKPVH--QLFDYICGVSTGAILAFML 492
Cdd:cd07214 1 GKFITVLSIDGGGIRGIIPatiLEFLEgKLQELDGPDARiaDYFDVIAGTSTGGLITAML 60
|
|
| Patatin_and_cPLA2 |
cd01819 |
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ... |
445-489 |
5.11e-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: 5.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 530386008 445 LSIDGGGTRGVVALQTLRKLVELTQkpvHQLFDYICGVSTGAILA 489
Cdd:cd01819 1 LSFSGGGFRGMYHAGVLSALAERGL---LDCVTYLAGTSGGAWVA 42
|
|
| |
