|
Name |
Accession |
Description |
Interval |
E-value |
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
15-373 |
0e+00 |
|
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: 590.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 15 KKILACDGGGILGLVSVEILTRLETDLRRELDQPELVLGDWFDFTCGTSTGAIIAACIAAGMSMARIGRFYTESGGQMFD 94
Cdd:cd07217 1 KKILALDGGGIRGLLSVEILGRIEKDLRTHLDDPEFRLGDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 95 RAALFKRLRYSYDDeplaaklRSEFDAALGHQPSTAEPHATLGSPALRTLLMMVMRNHSTDSPWPVCNNPDARYNDSGRR 174
Cdd:cd07217 81 KAWLAQRLFLNKLY-------NQYDPTNLGKKLNTVFPETTLGDDTLRTLLMIVTRNATTGSPWPVCNNPEAKYNDSDRS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 175 DCNLRLPLWQLVRASTAAPTFFPPEVVSFAEGTpqayRFVFVDGGVTTYNNPAFLAFQMATARPYAINWPTGTGQLLVVS 254
Cdd:cd07217 154 DCNLDLPLWQLVRASTAAPTFFPPEVVSIAPGT----AFVFVDGGVTTYNNPAFQAFLMATAKPYKLNWEVGADNLLLVS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 255 VGTGTAPRLRPDLQADDLWLLDHAKNIPGALMNAASAGWDMACRMLGECRHGGLLDREIGTMVSApgepPNWSGPKLFSY 334
Cdd:cd07217 230 VGTGFAPEARPDLKAADMWALDHAKYIPSALMNAANAGQDMVCRVLGECRKGGLVDREIGTMHVD----PNWLGPKLFTY 305
|
330 340 350
....*....|....*....|....*....|....*....
gi 500091471 335 VRYDPDVSRAGLDALGLSDVAEADVQRLDAIDRLPAIQR 373
Cdd:cd07217 306 VRYDVSLSRSGLDVLGLSDSQLEAVQKMDAVDQMEELQR 344
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
10-304 |
9.79e-53 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 177.40 E-value: 9.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 10 RRPGPKKILACDGGGILGLVSVEILTRLEtdlrRELDQPelvLGDWFDFTCGTSTGAIIAACIAAGMSMARIGRFYTESG 89
Cdd:COG3621 2 SANKPFRILSLDGGGIRGLIPARILAELE----ERLGKP---LAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 90 GQMFDRAALFKR------LRYSYDDEPLAAKLRSEFdaalghqpstaePHATLGSpaLRTLLMMVMRNHSTDSPWPVCNN 163
Cdd:COG3621 75 KEIFPKSRWRKLlslrglFGPKYDSEGLEKVLKEYF------------GDTTLGD--LKTPVLIPSYDLDNGKPVFFKSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 164 PDAryndsgrRDCNLRLPLWQLVRASTAAPTFFPPEVVSFAEGTpqayRFVFVDGGVTTyNNPAFLAFQMATArpyaiNW 243
Cdd:COG3621 141 HAK-------FDRDRDFLLVDVARATSAAPTYFPPAQIKNLTGE----GYALIDGGVFA-NNPALCALAEALK-----LL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500091471 244 PTGTGQLLVVSVGTGTAPRLRPDLQADDLWLLDHAKNIPGALMNAASAGWDMACRMLGECR 304
Cdd:COG3621 204 GPDLDDILVLSLGTGTAPRSIPYKKVKNWGALGWLLPLIDILMDAQSDAVDYQLRQLLGDR 264
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
18-231 |
1.50e-09 |
|
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: 57.23 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 18 LACDGGGILGLVSVEILTRLEtdlrRELDQPELVlgdwfdftCGTSTGAIIAACIAAGMSMARIGRFYTE---------- 87
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALG----EAGIRFDVI--------SGTSAGAINAALLALGRDPEEIEDLLLEldlnlflsli 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 88 --SGGQMFDRAALFKRLRYSYDDEPLAAKLRSEFDaalghqPSTAEPHATLGSPALRTLLMMVMRNHSTdspwpvcnNPD 165
Cdd:pfam01734 69 rkRALSLLALLRGLIGEGGLFDGDALRELLRKLLG------DLTLEELAARLSLLLVVALRALLTVIST--------ALG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500091471 166 ARYNDSGRRDCNLRLPLWQLVRASTAAPTFFPPEVVsfaEGTPqayrfvFVDGGVtTYNNPAFLAF 231
Cdd:pfam01734 135 TRARILLPDDLDDDEDLADAVLASSALPGVFPPVRL---DGEL------YVDGGL-VDNVPVEAAL 190
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
15-373 |
0e+00 |
|
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: 590.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 15 KKILACDGGGILGLVSVEILTRLETDLRRELDQPELVLGDWFDFTCGTSTGAIIAACIAAGMSMARIGRFYTESGGQMFD 94
Cdd:cd07217 1 KKILALDGGGIRGLLSVEILGRIEKDLRTHLDDPEFRLGDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLNGVNMFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 95 RAALFKRLRYSYDDeplaaklRSEFDAALGHQPSTAEPHATLGSPALRTLLMMVMRNHSTDSPWPVCNNPDARYNDSGRR 174
Cdd:cd07217 81 KAWLAQRLFLNKLY-------NQYDPTNLGKKLNTVFPETTLGDDTLRTLLMIVTRNATTGSPWPVCNNPEAKYNDSDRS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 175 DCNLRLPLWQLVRASTAAPTFFPPEVVSFAEGTpqayRFVFVDGGVTTYNNPAFLAFQMATARPYAINWPTGTGQLLVVS 254
Cdd:cd07217 154 DCNLDLPLWQLVRASTAAPTFFPPEVVSIAPGT----AFVFVDGGVTTYNNPAFQAFLMATAKPYKLNWEVGADNLLLVS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 255 VGTGTAPRLRPDLQADDLWLLDHAKNIPGALMNAASAGWDMACRMLGECRHGGLLDREIGTMVSApgepPNWSGPKLFSY 334
Cdd:cd07217 230 VGTGFAPEARPDLKAADMWALDHAKYIPSALMNAANAGQDMVCRVLGECRKGGLVDREIGTMHVD----PNWLGPKLFTY 305
|
330 340 350
....*....|....*....|....*....|....*....
gi 500091471 335 VRYDPDVSRAGLDALGLSDVAEADVQRLDAIDRLPAIQR 373
Cdd:cd07217 306 VRYDVSLSRSGLDVLGLSDSQLEAVQKMDAVDQMEELQR 344
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
10-304 |
9.79e-53 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 177.40 E-value: 9.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 10 RRPGPKKILACDGGGILGLVSVEILTRLEtdlrRELDQPelvLGDWFDFTCGTSTGAIIAACIAAGMSMARIGRFYTESG 89
Cdd:COG3621 2 SANKPFRILSLDGGGIRGLIPARILAELE----ERLGKP---LAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 90 GQMFDRAALFKR------LRYSYDDEPLAAKLRSEFdaalghqpstaePHATLGSpaLRTLLMMVMRNHSTDSPWPVCNN 163
Cdd:COG3621 75 KEIFPKSRWRKLlslrglFGPKYDSEGLEKVLKEYF------------GDTTLGD--LKTPVLIPSYDLDNGKPVFFKSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 164 PDAryndsgrRDCNLRLPLWQLVRASTAAPTFFPPEVVSFAEGTpqayRFVFVDGGVTTyNNPAFLAFQMATArpyaiNW 243
Cdd:COG3621 141 HAK-------FDRDRDFLLVDVARATSAAPTYFPPAQIKNLTGE----GYALIDGGVFA-NNPALCALAEALK-----LL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500091471 244 PTGTGQLLVVSVGTGTAPRLRPDLQADDLWLLDHAKNIPGALMNAASAGWDMACRMLGECR 304
Cdd:COG3621 204 GPDLDDILVLSLGTGTAPRSIPYKKVKNWGALGWLLPLIDILMDAQSDAVDYQLRQLLGDR 264
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
17-367 |
1.02e-41 |
|
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: 147.48 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 17 ILACDGGGILGLVSVEILTRLETDLRRELDqpelvLGDWFDFTCGTSTGAI-IAACIAAGMSMARIGRFYTESGGQMFDR 95
Cdd:cd07199 1 ILSLDGGGIRGIIPAEILAELEKRLGKPSR-----IADLFDLIAGTSTGGIiALGLALGRYSAEELVELYEELGRKIFPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 96 AALfkrlrYSYDDEplaaklrsefdaalghqpsTAEPHatlgspalrtllmmVMRNHstdspwpvcnnpdarynDSGRRD 175
Cdd:cd07199 76 VLV-----TAYDLS-------------------TGKPV--------------VFSNY-----------------DAEEPD 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 176 CNLRLPLWQLVRASTAAPTFFPPEVVSFAEGtpqayRFVFVDGGVtTYNNPAFLAFQMATArpyaiNWPTGTGQLLVVSV 255
Cdd:cd07199 101 DDDDFKLWDVARATSAAPTYFPPAVIESGGD-----EGAFVDGGV-AANNPALLALAEALR-----LLAPDKDDILVLSL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 256 GTGTAPRLRPDLQADDLWLLDHAKNIpGALMNAASAgwDMAcrmlgecrhggllDREIGTMVSAPGEPPNwsgpklfsYV 335
Cdd:cd07199 170 GTGTSPSSSSSKKASRWGGLGWGRPL-LDILMDAQS--DGV-------------DQWLDLLFGSLDSKDN--------YL 225
|
330 340 350
....*....|....*....|....*....|..
gi 500091471 336 RYDPDVSRAGLDalgLSDVAEADVQRLDAIDR 367
Cdd:cd07199 226 RINPPLPGPIPA---LDDASEANLLALDSAAF 254
|
|
| Pat17_PNPLA8_PNPLA9_like2 |
cd07215 |
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ... |
16-290 |
3.68e-25 |
|
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: 104.41 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 16 KILACDGGGILGLVSVEILTRLETDLRRELDQPELVLGDWFDFTCGTSTGA-------IIAACIAAGMSMARIGRFYTES 88
Cdd:cd07215 1 RILSIDGGGIRGIIPATILVSVEEKLQKKTGNPEARLADYFDLVAGTSTGGiltclylCPNESGRPKFSAKEALNFYLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 89 GGQMFDRAALFK-RLRYSYDDEPLAAKlrsEFDAALghqpstaepHATLGSPALRTLL---MMVMRNHSTDSPWpVCNNP 164
Cdd:cd07215 81 GNYIFKKKIWNKiKSRGGFLNEKYSHK---PLEEVL---------LEYFGDTKLSELLkpcLITSYDIERRSPH-FFKSH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 165 DARYNDSgrRDCNLRlplwQLVRASTAAPTFFPPEVVSFAEGTPqayrFVFVDGGVTTyNNPAFLAFQMATARPYAINWP 244
Cdd:cd07215 148 TAIKNEQ--RDFYVR----DVARATSAAPTYFEPARIHSLTGEK----YTLIDGGVFA-NNPTLCAYAEARKLKFEQPGK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 500091471 245 TGTGQLLVVSVGTGTAPRLRPDLQADDLWLLDHAKNIPGALMNAAS 290
Cdd:cd07215 217 PTAKDMIILSLGTGKNKKSYTYEKVKDWGLLGWAKPLIDIMMDGAS 262
|
|
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
7-261 |
9.60e-21 |
|
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: 91.55 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 7 ERIRRPGpKKILACDGGGILGLVSVEILTRLETDLRRELDQpelvlgdWFDFTCGTSTGA-IIAACIAAGMSMARIGRFY 85
Cdd:cd07211 1 PPVKGRG-IRILSIDGGGTRGVVALEILRKIEKLTGKPIHE-------LFDYICGVSTGAiLAFLLGLKKMSLDECEELY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 86 TESGGQMFDRAALF---KRLRYS---YDDEPLAAKLRSEFDAALGHQPStaephATLGSPALRTLLMMVmrNHSTDSPWP 159
Cdd:cd07211 73 RKLGKDVFSQNTYIsgtSRLVLShayYDTETWEKILKEMMGSDELIDTS-----ADPNCPKVACVSTQV--NRTPLKPYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 160 VCN-----NPDARYNDSgrrdCNLRlpLWQLVRASTAAPTFFPpevvSFAEGTpqayrFVFVDGGVTTyNNPAFLAfqMA 234
Cdd:cd07211 146 FRNynhppGTRSHYLGS----CKHK--LWEAIRASSAAPGYFE----EFKLGN-----NLHQDGGLLA-NNPTALA--LH 207
|
250 260
....*....|....*....|....*..
gi 500091471 235 TARPYainWPTGTGQlLVVSVGTGTAP 261
Cdd:cd07211 208 EAKLL---WPDTPIQ-CLVSVGTGRYP 230
|
|
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
17-260 |
1.72e-20 |
|
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: 91.73 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 17 ILACDGGGILGLVSVEILTRLETDLRrELDQPELVLGDWFDFTCGTSTGAIIAACIAAGMSMAR-------IGRFYTESG 89
Cdd:cd07214 6 VLSIDGGGIRGIIPATILEFLEGKLQ-ELDGPDARIADYFDVIAGTSTGGLITAMLTAPNENKRplfaakdIVQFYLENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 90 GQMF-----DRAALFKRLRYS----YDDEPLAAKLRSEFDAALGHQPSTaephaTLGSPALRTLLmmvmrnhstdspwpv 160
Cdd:cd07214 85 PKIFpqstgQFEDDRKKLRSLlgpkYDGVYLHDLLNELLGDTRLSDTLT-----NVVIPTFDIKL--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 161 cNNPDARYNDSGRRDCNLRLPLWQLVRASTAAPTFFPPEVVSFAEGTPQAYRFVFVDGGVTTyNNPAFLAFQMAT----- 235
Cdd:cd07214 145 -LQPVIFSSSKAKNDKLTNARLADVCISTSAAPTYFPAHYFTTEDSNGDIREFNLVDGGVAA-NNPTLLAISEVTkeiik 222
|
250 260
....*....|....*....|....*..
gi 500091471 236 --ARPYAINwPTGTGQLLVVSVGTGTA 260
Cdd:cd07214 223 dnPFFASIK-PLDYKKLLVLSLGTGSA 248
|
|
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
17-261 |
7.78e-15 |
|
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: 74.68 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 17 ILACDGGGILGLVSVEILTRLEtdlrRELDQPelvLGDWFDFTCGTSTGAIIAACIAAGMSMARIGRFYTesggQMFDRa 96
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIE----KALGRP---IRELFDWIAGTSTGGILALALLHGKSLREARRLYL----RMKDR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 97 aLFKRLRySYDDEPLAAKLRSEFDAalgHQPSTAEPH------ATLGSPALRTLLMmvMRNH---STDSPWPVcNNPDAR 167
Cdd:cd07212 69 -VFDGSR-PYNSEPLEEFLKREFGE---DTKMTDVKYprlmvtGVLADRQPVQLHL--FRNYdppEDVEEPEK-NANFLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 168 YNDSgrrdcnLRLPLWQLVRASTAAPTFFPPevvsFAEgtpqayrfvFVDGGVTTyNNPAF-----LAFQMATARPYAI- 241
Cdd:cd07212 141 PTDP------AEQLLWRAARSSGAAPTYFRP----MGR---------FLDGGLIA-NNPTLdamteIHEYNKTLKSKGRk 200
|
250 260
....*....|....*....|..
gi 500091471 242 --NWPTGtgqlLVVSVGTGTAP 261
Cdd:cd07212 201 nkVKKIG----CVVSLGTGIIP 218
|
|
| Pat17_PNPLA8_PNPLA9_like1 |
cd07213 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
16-304 |
2.13e-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: 70.01 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 16 KILACDGGGILGLVSVEILTRLETDLRRELDQPELVlgdwfdftCGTSTGAIIAACIAAGMSMARIGRFYTESGGQMFDR 95
Cdd:cd07213 3 RILSLDGGGVKGIVQLVLLKRLAEEFPSFLDQIDLF--------AGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 96 aalfkrlrysyddeplaaklRSEFDAALGHQPSTAEPHATLGS--PALRTLlmmvmrnhsTDSPWPVCNNP---DARYND 170
Cdd:cd07213 75 --------------------SSAGGGAGNNQYFAAGFLKAFAEvfFGDLTL---------GDLKRKVLVPSfqlDSGKDD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 171 SGRR-----------DCNLRLPLWQLVRASTAAPTFFPPEvvsfaegtpQAYrfvfVDGGVTTyNNPAFLAFqmatarPY 239
Cdd:cd07213 126 PNRRwkpklfhnfpgEPDLDELLVDVCLRSSAAPTYFPSY---------QGY----VDGGVFA-NNPSLCAI------AQ 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 240 AINwPTGTG----QLLVVSVGTGTAP-RLRPDLQADDLWLLDHAKNIPGALMNAASAGWDMACRMLGECR 304
Cdd:cd07213 186 AIG-EEGLNidlkDIVVLSLGTGRPPsYLDGANGYGDWGLLQWLPDLLDLFMDAGVDAADFQCRQLLGER 254
|
|
| Pat17_PNPLA8_PNPLA9_like3 |
cd07216 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
15-261 |
4.15e-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: 132855 [Multi-domain] Cd Length: 309 Bit Score: 69.25 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 15 KKILACDGGGILGLVSVEILTRL--ETDLRRELDQPeLVLGDWFDFTCGTSTGaiiaaciaaGMSMARIGRF-------- 84
Cdd:cd07216 1 LNLLSLDGGGVRGLSSLLILKEImeRIDPKEGLDEP-PKPCDYFDLIGGTSTG---------GLIAIMLGRLrmtvdeci 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 85 --YTESGGQMFDRaalfKRLRYSYDDEPLAAKLRSEFDAA--------LGHQPSTAE-PHATLGS-------PALRTLLM 146
Cdd:cd07216 71 daYTRLAKKIFSR----KRLRLIIGDLRTGARFDSKKLAEaikvilkeLGNDEDDLLdEGEEDGCkvfvcatDKDVTGKA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 147 MVMRNHSTdspwpvcnnpdaRYNDSGRRDCnlrlPLWQLVRASTAAPTFFPPEVVSFAEGTpqayrfvFVDGGvTTYNNP 226
Cdd:cd07216 147 VRLRSYPS------------KDEPSLYKNA----TIWEAARATSAAPTFFDPVKIGPGGRT-------FVDGG-LGANNP 202
|
250 260 270
....*....|....*....|....*....|....*.
gi 500091471 227 AFLAFQMATArpyaiNWPTGTGQL-LVVSVGTGTAP 261
Cdd:cd07216 203 IREVWSEAVS-----LWEGLARLVgCLVSIGTGTPS 233
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
18-231 |
1.50e-09 |
|
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: 57.23 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 18 LACDGGGILGLVSVEILTRLEtdlrRELDQPELVlgdwfdftCGTSTGAIIAACIAAGMSMARIGRFYTE---------- 87
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALG----EAGIRFDVI--------SGTSAGAINAALLALGRDPEEIEDLLLEldlnlflsli 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091471 88 --SGGQMFDRAALFKRLRYSYDDEPLAAKLRSEFDaalghqPSTAEPHATLGSPALRTLLMMVMRNHSTdspwpvcnNPD 165
Cdd:pfam01734 69 rkRALSLLALLRGLIGEGGLFDGDALRELLRKLLG------DLTLEELAARLSLLLVVALRALLTVIST--------ALG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500091471 166 ARYNDSGRRDCNLRLPLWQLVRASTAAPTFFPPEVVsfaEGTPqayrfvFVDGGVtTYNNPAFLAF 231
Cdd:pfam01734 135 TRARILLPDDLDDDEDLADAVLASSALPGVFPPVRL---DGEL------YVDGGL-VDNVPVEAAL 190
|
|
| RssA |
COG1752 |
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
181-242 |
8.38e-03 |
|
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];
Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 37.57 E-value: 8.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500091471 181 PLWQLVRASTAAPTFFPPEVVsfaEGTpqayrfVFVDGGVTtyNN-PAFLAFQMATARPYAIN 242
Cdd:COG1752 138 PLADAVRASAAIPGVFPPVEI---DGR------LYVDGGVV--NNlPVDPARALGADRVIAVD 189
|
|
| |
