|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
176-502 |
6.17e-154 |
|
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: 442.93 E-value: 6.17e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 176 LLALDGGGIRAVITIQMLIHIDYLLGGKLVEKLDDIAGTSCGGVITLLLSTNnRNIEETRKLLLDMRDRVFIRGadkaVP 255
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHG-KSLREARRLYLRMKDRVFDGS----RP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 256 KYSSNGMEYIARHVTTWedSKMSSIKRHRAIVTVADTRMVPPQLLLFRSYRPEMPEEACE----HYKFLDPTKVELWKTL 331
Cdd:cd07212 76 YNSEPLEEFLKREFGED--TKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEknanFLPPTDPAEQLLWRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 332 RCTTAAPYFFESFNGLSDGGLIANNPTLALISDFFLTNKLEKSFakssseRENRGNWKIGCVISLGTGVFPTEKIDGIDl 411
Cdd:cd07212 154 RSSGAAPTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSK------GRKNKVKKIGCVVSLGTGIIPQTPVNTVD- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 412 iVAHAKNPIQFAKScykaFASTRNLLHVLVKECTASNGQPVRYAREWCHSINAPYFRFSPHLSQGISLDEIDLEKVMQVM 491
Cdd:cd07212 227 -VFRPSNPWELAKT----VFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNML 301
|
330
....*....|.
gi 392885195 492 WETEQYVASHR 502
Cdd:cd07212 302 WDTEVYIYTHR 312
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
177-493 |
2.36e-28 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 114.62 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLIHIDYLLGGKLVEKLDDIAGTSCGGVITLLLSTnNRNIEETRKLLLDMRDRVFIRGADKAV-- 254
Cdd:COG3621 10 LSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRKLls 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 255 ------PKYSSNGMEYIARHVTtwEDSKMSSIKRHRAIVTV-ADTRmvppQLLLFRSYRPemPEEACEHYKfldptkveL 327
Cdd:COG3621 89 lrglfgPKYDSEGLEKVLKEYF--GDTTLGDLKTPVLIPSYdLDNG----KPVFFKSPHA--KFDRDRDFL--------L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 328 WKTLRCTTAAPYFFESFN---------GLSDGGLIANNPTLALISDffltnkLEKSFAKSSSEREnrgnwkigcVISLGT 398
Cdd:COG3621 153 VDVARATSAAPTYFPPAQiknltgegyALIDGGVFANNPALCALAE------ALKLLGPDLDDIL---------VLSLGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 399 GvfptekidgidlivaHAKNPIQFAKSCYK-AFASTRNLLHVLvkecTASNGQPVRYareWCHSINAP-YFRFSPHLSQG 476
Cdd:COG3621 218 G---------------TAPRSIPYKKVKNWgALGWLLPLIDIL----MDAQSDAVDY---QLRQLLGDrYYRLDPELPEE 275
|
330
....*....|....*..
gi 392885195 477 ISLDeiDLEKVMQVMWE 493
Cdd:COG3621 276 IALD--DNAENIEALLA 290
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
177-362 |
3.21e-14 |
|
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: 71.10 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLihiDYLlgGKLVEKLDDIAGTSCGGVITLLLSTnNRNIEETRKLLLDMRDRVFIRGADKAVPK 256
Cdd:pfam01734 1 LVLSGGGARGAYHLGVL---KAL--GEAGIRFDVISGTSAGAINAALLAL-GRDPEEIEDLLLELDLNLFLSLIRKRALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 257 YSSNGMEYIARH-------VTTWEDSKMSSIKRHRAIVTVADTRMVPPQLLLFRSYRPEmPEEACEHYKFLDPTKVELWK 329
Cdd:pfam01734 75 LLALLRGLIGEGglfdgdaLRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTAL-GTRARILLPDDLDDDEDLAD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 392885195 330 TLRCTTAAPYFFE--SFNG--LSDGGLIANNPTLALI 362
Cdd:pfam01734 154 AVLASSALPGVFPpvRLDGelYVDGGLVDNVPVEAAL 190
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
56-105 |
1.57e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.12 E-value: 1.57e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392885195 56 LMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLV 105
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
177-359 |
2.14e-09 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 59.05 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLIHIDYLLGGKLVEKLDDIAGTSCGGVITLLLSTNN--RNIEET-----------RKLLldmrd 243
Cdd:NF041079 4 LSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIpaRELVELfeehgkdifpkRKWP----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 244 RVFIRGADKavPKYSSNGMeyiARHVTTW-EDSKMSSIKrHRAI---VTVADTRmvpPQllLFRSyrPEMPE-EACEHYK 318
Cdd:NF041079 79 RRLLGLLKK--PKYSSEPL---REVLEEIfGDKTIGDLK-HRVLipaVNYTTGK---PQ--VFKT--PHHPDfTRDHKLK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392885195 319 FLDptkVELwktlrCTTAAPYFFE-SFNGLS---DGGLIANNPTL 359
Cdd:NF041079 146 LVD---VAL-----ATSAAPTYFPlHEFDNEqfvDGGLVANNPGL 182
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
55-123 |
6.42e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 51.11 E-value: 6.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392885195 55 ALMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLVVLCApcqIWKIKNNNGLT 123
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKT 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
176-502 |
6.17e-154 |
|
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: 442.93 E-value: 6.17e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 176 LLALDGGGIRAVITIQMLIHIDYLLGGKLVEKLDDIAGTSCGGVITLLLSTNnRNIEETRKLLLDMRDRVFIRGadkaVP 255
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHG-KSLREARRLYLRMKDRVFDGS----RP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 256 KYSSNGMEYIARHVTTWedSKMSSIKRHRAIVTVADTRMVPPQLLLFRSYRPEMPEEACE----HYKFLDPTKVELWKTL 331
Cdd:cd07212 76 YNSEPLEEFLKREFGED--TKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEknanFLPPTDPAEQLLWRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 332 RCTTAAPYFFESFNGLSDGGLIANNPTLALISDFFLTNKLEKSFakssseRENRGNWKIGCVISLGTGVFPTEKIDGIDl 411
Cdd:cd07212 154 RSSGAAPTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSK------GRKNKVKKIGCVVSLGTGIIPQTPVNTVD- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 412 iVAHAKNPIQFAKScykaFASTRNLLHVLVKECTASNGQPVRYAREWCHSINAPYFRFSPHLSQGISLDEIDLEKVMQVM 491
Cdd:cd07212 227 -VFRPSNPWELAKT----VFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNML 301
|
330
....*....|.
gi 392885195 492 WETEQYVASHR 502
Cdd:cd07212 302 WDTEVYIYTHR 312
|
|
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
174-498 |
9.03e-37 |
|
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: 138.54 E-value: 9.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 174 RVLlALDGGGIRAVITIQMLIHIDYLLGGKLVEKLDDIAGTSCGGVITLLLSTNNRNIEETRKLLLDMRDRVFIR----- 248
Cdd:cd07211 9 RIL-SIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLKKMSLDECEELYRKLGKDVFSQntyis 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 249 GADKAV---PKYSSNGMEYIAR----HVTTWEDSKMSSIKRHRAIVTVADTrmVPPQLLLFRSYrpEMPEEACEHYkfLD 321
Cdd:cd07211 88 GTSRLVlshAYYDTETWEKILKemmgSDELIDTSADPNCPKVACVSTQVNR--TPLKPYVFRNY--NHPPGTRSHY--LG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 322 PTKVELWKTLRCTTAAPYFFESF----NGLSDGGLIANNPT-LALisdffltnkleksfakssseRENRGNW---KIGCV 393
Cdd:cd07211 162 SCKHKLWEAIRASSAAPGYFEEFklgnNLHQDGGLLANNPTaLAL--------------------HEAKLLWpdtPIQCL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 394 ISLGTGVFPTEKIDGIDLIVAhaknpiqFAKSCYKAFAS------TRNLLHVLVKECTasngqpvryarewchsinapYF 467
Cdd:cd07211 222 VSVGTGRYPSSVRLETGGYTS-------LKTKLLNLIDSatdterVHTALDDLLPPDV--------------------YF 274
|
330 340 350
....*....|....*....|....*....|.
gi 392885195 468 RFSPHLSQGISLDEIDLEKVMQVMWETEQYV 498
Cdd:cd07211 275 RFNPVMSECVELDETRPEKLDQLQDDTLEYI 305
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
177-493 |
2.36e-28 |
|
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only];
Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 114.62 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLIHIDYLLGGKLVEKLDDIAGTSCGGVITLLLSTnNRNIEETRKLLLDMRDRVFIRGADKAV-- 254
Cdd:COG3621 10 LSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAA-GYSAEEILDLYEEEGKEIFPKSRWRKLls 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 255 ------PKYSSNGMEYIARHVTtwEDSKMSSIKRHRAIVTV-ADTRmvppQLLLFRSYRPemPEEACEHYKfldptkveL 327
Cdd:COG3621 89 lrglfgPKYDSEGLEKVLKEYF--GDTTLGDLKTPVLIPSYdLDNG----KPVFFKSPHA--KFDRDRDFL--------L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 328 WKTLRCTTAAPYFFESFN---------GLSDGGLIANNPTLALISDffltnkLEKSFAKSSSEREnrgnwkigcVISLGT 398
Cdd:COG3621 153 VDVARATSAAPTYFPPAQiknltgegyALIDGGVFANNPALCALAE------ALKLLGPDLDDIL---------VLSLGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 399 GvfptekidgidlivaHAKNPIQFAKSCYK-AFASTRNLLHVLvkecTASNGQPVRYareWCHSINAP-YFRFSPHLSQG 476
Cdd:COG3621 218 G---------------TAPRSIPYKKVKNWgALGWLLPLIDIL----MDAQSDAVDY---QLRQLLGDrYYRLDPELPEE 275
|
330
....*....|....*..
gi 392885195 477 ISLDeiDLEKVMQVMWE 493
Cdd:COG3621 276 IALD--DNAENIEALLA 290
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
177-497 |
4.60e-26 |
|
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: 107.42 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLIHIDYLLGGK--LVEKLDDIAGTSCGGVITLLLSTNNRNIEETRKLLLDMRDRVFirgadkav 254
Cdd:cd07199 2 LSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGRYSAEELVELYEELGRKIF-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 255 pkyssngmeyiarhvttwedskmssikrHRAIVTVadTRMVPPQLLLFRSYRpempeeaceHYKFLDPTKVELWKTLRCT 334
Cdd:cd07199 74 ----------------------------PRVLVTA--YDLSTGKPVVFSNYD---------AEEPDDDDDFKLWDVARAT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 335 TAAPYFFESFNGLS--------DGGLIANNPTLAlisdffltnkleksfAKSSSERENRGNWKIGCVISLGTGVFPteki 406
Cdd:cd07199 115 SAAPTYFPPAVIESggdegafvDGGVAANNPALL---------------ALAEALRLLAPDKDDILVLSLGTGTSP---- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 407 DGIDLIVAHAKNPIQfakscykafaSTRNLLHVLVKECTASngqpvryAREWCHSINAP------YFRFSPHLSQGIS-L 479
Cdd:cd07199 176 SSSSSKKASRWGGLG----------WGRPLLDILMDAQSDG-------VDQWLDLLFGSldskdnYLRINPPLPGPIPaL 238
|
330
....*....|....*...
gi 392885195 480 DEIDLEKVMQVMWETEQY 497
Cdd:cd07199 239 DDASEANLLALDSAAFEL 256
|
|
| Pat17_PNPLA8_PNPLA9_like3 |
cd07216 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
176-499 |
3.17e-17 |
|
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: 82.74 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 176 LLALDGGGIR---AVITIQMLIH-IDYLLGGKLVEK----LDDIAGTSCGGVITLLLS----TNNRNIEE---------- 233
Cdd:cd07216 3 LLSLDGGGVRglsSLLILKEIMErIDPKEGLDEPPKpcdyFDLIGGTSTGGLIAIMLGrlrmTVDECIDAytrlakkifs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 234 TRKLLLDMRDRVFIRGAD--------KAVPKYSSNgmeyiarhvTTWEDSKMSSIKRHRAIVTVadTRMVPPQLL-LFRS 304
Cdd:cd07216 83 RKRLRLIIGDLRTGARFDskklaeaiKVILKELGN---------DEDDLLDEGEEDGCKVFVCA--TDKDVTGKAvRLRS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 305 YRPEMPEEaceHYKfldptKVELWKTLRCTTAAPYFFESFN------GLSDGGLIANNPTLALISDffltnkleksfAKS 378
Cdd:cd07216 152 YPSKDEPS---LYK-----NATIWEAARATSAAPTFFDPVKigpggrTFVDGGLGANNPIREVWSE-----------AVS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 379 SSERENRgnwKIGCVISLGTGVFPTEKIDGIDLIVahaknpiqFAKSCYKAFASTRNLLHVLVKECTASNGQPVRyarew 458
Cdd:cd07216 213 LWEGLAR---LVGCLVSIGTGTPSIKSLGRSAEGA--------GLLKGLKDLVTDTEAEAKRFSAEHSELDEEGR----- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 392885195 459 chsinapYFRFS-PHLSQGISLDEIDLEKVMQVMweTEQYVA 499
Cdd:cd07216 277 -------YFRFNvPHGLEDVGLDEYEKMEEIVSL--TREYLA 309
|
|
| Pat17_PNPLA8_PNPLA9_like1 |
cd07213 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
177-490 |
1.26e-15 |
|
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: 77.33 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLIHIDYlLGGKLVEKLDDIAGTSCGGVITLLLSTnNRNIEETRKLLLDMRDRVF---IRGADKA 253
Cdd:cd07213 5 LSLDGGGVKGIVQLVLLKRLAE-EFPSFLDQIDLFAGTSAGSLIALGLAL-GYSPRQVLKLYEEVGLKVFsksSAGGGAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 254 VPKYSSNGMEYIARHVtTWEDSKMSSIKRHRAIVTVA-DTRMVPPQlllfRSYRPEM----PEEACEHYKFLDptkvelw 328
Cdd:cd07213 83 NNQYFAAGFLKAFAEV-FFGDLTLGDLKRKVLVPSFQlDSGKDDPN----RRWKPKLfhnfPGEPDLDELLVD------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 329 KTLRcTTAAPYFFESFNGLSDGGLIANNPTLA----LISDFFLTNKLEKSfakssserenrgnwkigCVISLGTGvFPTE 404
Cdd:cd07213 151 VCLR-SSAAPTYFPSYQGYVDGGVFANNPSLCaiaqAIGEEGLNIDLKDI-----------------VVLSLGTG-RPPS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 405 KIDGIDLIvaHAKNPIQFAKSCYKAFASTRnllhvlvkectasngqpVRYAREWCHSINAP-YFRFSPHLSQGISLDEI- 482
Cdd:cd07213 212 YLDGANGY--GDWGLLQWLPDLLDLFMDAG-----------------VDAADFQCRQLLGErYFRLDPVLPANIDLDDNk 272
|
....*...
gi 392885195 483 DLEKVMQV 490
Cdd:cd07213 273 QIEELVEI 280
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
177-362 |
3.21e-14 |
|
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: 71.10 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLihiDYLlgGKLVEKLDDIAGTSCGGVITLLLSTnNRNIEETRKLLLDMRDRVFIRGADKAVPK 256
Cdd:pfam01734 1 LVLSGGGARGAYHLGVL---KAL--GEAGIRFDVISGTSAGAINAALLAL-GRDPEEIEDLLLELDLNLFLSLIRKRALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 257 YSSNGMEYIARH-------VTTWEDSKMSSIKRHRAIVTVADTRMVPPQLLLFRSYRPEmPEEACEHYKFLDPTKVELWK 329
Cdd:pfam01734 75 LLALLRGLIGEGglfdgdaLRELLRKLLGDLTLEELAARLSLLLVVALRALLTVISTAL-GTRARILLPDDLDDDEDLAD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 392885195 330 TLRCTTAAPYFFE--SFNG--LSDGGLIANNPTLALI 362
Cdd:pfam01734 154 AVLASSALPGVFPpvRLDGelYVDGGLVDNVPVEAAL 190
|
|
| Pat17_PNPLA8_PNPLA9_like2 |
cd07215 |
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ... |
176-512 |
2.04e-12 |
|
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: 68.59 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 176 LLALDGGGIRAVITIQMLIHIDYLLGGK-------LVEKLDDIAGTSCGGVITLL-LSTNNRNI-----EETRKLLLDMR 242
Cdd:cd07215 2 ILSIDGGGIRGIIPATILVSVEEKLQKKtgnpearLADYFDLVAGTSTGGILTCLyLCPNESGRpkfsaKEALNFYLERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 243 DRVFIRGADKAV--------PKYSSNGMEYIARHVttWEDSKMSSIKRhRAIVTVADTRMVPPQllLFRSYRPEMPEEac 314
Cdd:cd07215 82 NYIFKKKIWNKIksrggflnEKYSHKPLEEVLLEY--FGDTKLSELLK-PCLITSYDIERRSPH--FFKSHTAIKNEQ-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 315 ehYKFLdptkveLWKTLRCTTAAPYFFE-----SFNG----LSDGGLIANNPTLALISDF--FLTNKLEKSFAKSSsere 383
Cdd:cd07215 155 --RDFY------VRDVARATSAAPTYFEparihSLTGekytLIDGGVFANNPTLCAYAEArkLKFEQPGKPTAKDM---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 384 nrgnwkigCVISLGTG----VFPTEKidgidlivahAKN--PIQFAKScykafastrnLLHVLVKectaSNGQPVRYARE 457
Cdd:cd07215 223 --------IILSLGTGknkkSYTYEK----------VKDwgLLGWAKP----------LIDIMMD----GASQTVDYQLK 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 392885195 458 WCH-SINAP--YFRFSPHLSQGIS-LDEIDLEKVMQVMWETEQYVASHRPQFVKLVNYL 512
Cdd:cd07215 271 QIFdAEGDQqqYLRIQPELEDADPeMDDASPENLEKLREVGQALAEDHKDQLDEIVDRL 329
|
|
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
176-399 |
5.75e-11 |
|
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: 64.00 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 176 LLALDGGGIRAVITIQMLIHIDYLLGG------KLVEKLDDIAGTSCGGVITLLLSTNNRN------IEETRKLLLDMRD 243
Cdd:cd07214 6 VLSIDGGGIRGIIPATILEFLEGKLQEldgpdaRIADYFDVIAGTSTGGLITAMLTAPNENkrplfaAKDIVQFYLENGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 244 RVF-----IRGADKAVPKYsSNGMEYIARHVTTWEDSKMSSIKRHRA----IVTVADTRMVPPqlLLFRSYrpEMPEEAC 314
Cdd:cd07214 86 KIFpqstgQFEDDRKKLRS-LLGPKYDGVYLHDLLNELLGDTRLSDTltnvVIPTFDIKLLQP--VIFSSS--KAKNDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 315 EHYKFLDptkvelwkTLRCTTAAPYFF--------------ESFNgLSDGGLIANNPTLALISDffLTNKLEKSFAKSSS 380
Cdd:cd07214 161 TNARLAD--------VCISTSAAPTYFpahyfttedsngdiREFN-LVDGGVAANNPTLLAISE--VTKEIIKDNPFFAS 229
|
250
....*....|....*....
gi 392885195 381 ERENrgNWKIGCVISLGTG 399
Cdd:cd07214 230 IKPL--DYKKLLVLSLGTG 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
56-105 |
1.57e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.12 E-value: 1.57e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392885195 56 LMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLV 105
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
177-359 |
2.14e-09 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 59.05 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 177 LALDGGGIRAVITIQMLIHIDYLLGGKLVEKLDDIAGTSCGGVITLLLSTNN--RNIEET-----------RKLLldmrd 243
Cdd:NF041079 4 LSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIpaRELVELfeehgkdifpkRKWP----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 244 RVFIRGADKavPKYSSNGMeyiARHVTTW-EDSKMSSIKrHRAI---VTVADTRmvpPQllLFRSyrPEMPE-EACEHYK 318
Cdd:NF041079 79 RRLLGLLKK--PKYSSEPL---REVLEEIfGDKTIGDLK-HRVLipaVNYTTGK---PQ--VFKT--PHHPDfTRDHKLK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392885195 319 FLDptkVELwktlrCTTAAPYFFE-SFNGLS---DGGLIANNPTL 359
Cdd:NF041079 146 LVD---VAL-----ATSAAPTYFPlHEFDNEqfvDGGLVANNPGL 182
|
|
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
176-496 |
1.02e-08 |
|
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: 57.12 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 176 LLALDGGGIRAVITIQMLIHI-----------DYLLGgklvEKLDDIAGTSCGGVITLLLS-------------TNNRNI 231
Cdd:cd07217 3 ILALDGGGIRGLLSVEILGRIekdlrthlddpEFRLG----DYFDFVGGTSTGSIIAACIAlgmsvtdllsfytLNGVNM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 232 EETRKLLLDMRDRVFIRGADKAVPKYSSNgmeYIARHVTTWEDS----KMSSIKRHraivTVADTRMVP--PQLLLFRSY 305
Cdd:cd07217 79 FDKAWLAQRLFLNKLYNQYDPTNLGKKLN---TVFPETTLGDDTlrtlLMIVTRNA----TTGSPWPVCnnPEAKYNDSD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 306 RpempeeaceHYKFLDptkVELWKTLRCTTAAPYFFE----SFNG-----LSDGGL-IANNPTLALisdfFLTnkleksf 375
Cdd:cd07217 152 R---------SDCNLD---LPLWQLVRASTAAPTFFPpevvSIAPgtafvFVDGGVtTYNNPAFQA----FLM------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885195 376 aksSSERENRGNWKIGC----VISLGTGVFPTEKIDG--IDL-IVAHAKN---PIQFAkscykAFASTRNLLHVLvKECT 445
Cdd:cd07217 209 ---ATAKPYKLNWEVGAdnllLVSVGTGFAPEARPDLkaADMwALDHAKYipsALMNA-----ANAGQDMVCRVL-GECR 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392885195 446 ASN------GQPvRYAREWCHSINAPYFRFSPHLSQGiSLDEIDL----EKVMQVMWETEQ 496
Cdd:cd07217 280 KGGlvdreiGTM-HVDPNWLGPKLFTYVRYDVSLSRS-GLDVLGLsdsqLEAVQKMDAVDQ 338
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
50-105 |
2.76e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 51.27 E-value: 2.76e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 392885195 50 CNHLEALMNAARYGNTDLLyKLYIHHIDLRMTDEtGNTAMHVAVMNNQQKIVRMLV 105
Cdd:pfam12796 28 KNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLL 81
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
52-105 |
3.36e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 3.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 392885195 52 HLEALMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLV 105
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
55-123 |
6.42e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 51.11 E-value: 6.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392885195 55 ALMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLVVLCApcqIWKIKNNNGLT 123
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKT 221
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
55-123 |
1.76e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 49.95 E-value: 1.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392885195 55 ALMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLvvLCAPCQIwKIKNNNGLT 123
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL--LEAGADV-NARDNDGET 188
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
55-105 |
2.61e-05 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 46.10 E-value: 2.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 392885195 55 ALMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLV 105
Cdd:COG0666 90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
55-122 |
1.57e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 43.79 E-value: 1.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392885195 55 ALMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVAVMNNQQKIVRMLVVLCAPCQIWKIKNNNGL 122
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
54-92 |
1.82e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 1.82e-04
10 20 30
....*....|....*....|....*....|....*....
gi 392885195 54 EALMNAARYGNTDLLYKLYIHHIDLRMTDETGNTAMHVA 92
Cdd:pfam13857 18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| |
