|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
141-455 |
1.26e-166 |
|
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: 472.97 E-value: 1.26e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNnqkfPKH 220
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGS----RPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 221 SALGIETCLQEVMGSKTLMSKCTAHRLVVTTAKVTLAPPQLVLFRSYAPRIDSKEFE----QLGYFNPNKILLWKAIRCT 296
Cdd:cd07212 77 NSEPLEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEknanFLPPTDPAEQLLWRAARSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 297 TAAPTYFPSFNGMADGALFCNNPCIMVMTEFAKLKKIENYRG-KNNTDEIGCVISVGTGIEPSYPINGIDINLTSGLtgi 375
Cdd:cd07212 157 GAAPTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGrKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNP--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 376 tGNWREIIENTKNLITVFLYQCTSSHNVHVGQSREWCHSMQVPFFRFSPHLAAPFELDNCKIEDITNAMFDNEVYIRTEI 455
Cdd:cd07212 234 -WELAKTVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
141-433 |
2.23e-38 |
|
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: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNNQKF--- 217
Cdd:COG3621 9 ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIFPKSRWRKlls 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 218 ------PKHSALGIETCLQEVMGSKTLmSKCTaHRLVVTTAKVTLAPPqlVLFRSYAPRIDskefeqlgyfNPNKILLWK 291
Cdd:COG3621 89 lrglfgPKYDSEGLEKVLKEYFGDTTL-GDLK-TPVLIPSYDLDNGKP--VFFKSPHAKFD----------RDRDFLLVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 292 AIRCTTAAPTYFPSFN---------GMADGALFCNNP--CIMVMTEFAKLKKIENYRgknntdeigcVISVGTGIEP-SY 359
Cdd:COG3621 155 VARATSAAPTYFPPAQiknltgegyALIDGGVFANNPalCALAEALKLLGPDLDDIL----------VLSLGTGTAPrSI 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899743 360 PINGIDinltsgltgitgNWReIIENTKNLITVFLYqcTSSHNVHvGQSRewcHSMQVPFFRFSPHLAAPFELD 433
Cdd:COG3621 225 PYKKVK------------NWG-ALGWLLPLIDILMD--AQSDAVD-YQLR---QLLGDRYYRLDPELPEEIALD 279
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
141-353 |
4.31e-19 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 87.94 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNNQ----- 215
Cdd:NF041079 3 ILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKWprrll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 216 ---KFPKHSALGIETCLQEVMGSKTLmSKCTaHRLVVTTAKVTLAPPQlvLFRSyaPRidSKEFEQlgyfnPNKILLWKA 292
Cdd:NF041079 83 gllKKPKYSSEPLREVLEEIFGDKTI-GDLK-HRVLIPAVNYTTGKPQ--VFKT--PH--HPDFTR-----DHKLKLVDV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899743 293 IRCTTAAPTYFP--SFNG--MADGALFCNNPCIMVMTE---FAKlKKIENYRgknntdeigcVISVGT 353
Cdd:NF041079 150 ALATSAAPTYFPlhEFDNeqFVDGGLVANNPGLLGLHEalhFLG-VPYDDVR----------ILSIGT 206
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
142-319 |
1.85e-13 |
|
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: 68.79 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 142 LSLDGGGLRVVLQCAILLAVERELGEPLRnrihwIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNNQKFPKHS 221
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIRFDV-----ISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 222 ALGIETC---------------LQEVMGSKTLMSKCTAHRLVVTTAKVTLAPPQLVLFRSYAPRIDSKEFEqlgyfnpNK 286
Cdd:pfam01734 76 LALLRGLigegglfdgdalrelLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLD-------DD 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 392899743 287 ILLWKAIRCTTAAPTYFP--SFNG--MADGALFCNNP 319
Cdd:pfam01734 149 EDLADAVLASSALPGVFPpvRLDGelYVDGGLVDNVP 185
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
9-89 |
6.27e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 41.86 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 9 INAQEIYKRHIdIFHAITYDNIDgLVAAFV-RNEPFDIKDKNGNTPLHLAAKLNR----RLLCravcvyAAGLDLwNSKN 83
Cdd:COG0666 113 VNARDKDGETP-LHLAAYNGNLE-IVKLLLeAGADVNAQDNDGNTPLHLAAANGNleivKLLL------EAGADV-NARD 183
|
....*.
gi 392899743 84 NDGKTP 89
Cdd:COG0666 184 NDGETP 189
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
44-92 |
2.29e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 2.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392899743 44 DIKDKNGNTPLHLAAKLNRRLLCRAVCVYaaGLDlWNSKNNDGKTPIEM 92
Cdd:pfam13857 10 NRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVD-LNLKDEEGLTALDL 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pat_PNPLA9 |
cd07212 |
Patatin-like phospholipase domain containing protein 9; PNPLA9 is a Ca-independent ... |
141-455 |
1.26e-166 |
|
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: 472.97 E-value: 1.26e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNnqkfPKH 220
Cdd:cd07212 1 LLCLDGGGIRGLVLIQMLIAIEKALGRPIRELFDWIAGTSTGGILALALLHGKSLREARRLYLRMKDRVFDGS----RPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 221 SALGIETCLQEVMGSKTLMSKCTAHRLVVTTAKVTLAPPQLVLFRSYAPRIDSKEFE----QLGYFNPNKILLWKAIRCT 296
Cdd:cd07212 77 NSEPLEEFLKREFGEDTKMTDVKYPRLMVTGVLADRQPVQLHLFRNYDPPEDVEEPEknanFLPPTDPAEQLLWRAARSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 297 TAAPTYFPSFNGMADGALFCNNPCIMVMTEFAKLKKIENYRG-KNNTDEIGCVISVGTGIEPSYPINGIDINLTSGLtgi 375
Cdd:cd07212 157 GAAPTYFRPMGRFLDGGLIANNPTLDAMTEIHEYNKTLKSKGrKNKVKKIGCVVSLGTGIIPQTPVNTVDVFRPSNP--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 376 tGNWREIIENTKNLITVFLYQCTSSHNVHVGQSREWCHSMQVPFFRFSPHLAAPFELDNCKIEDITNAMFDNEVYIRTEI 455
Cdd:cd07212 234 -WELAKTVFGAKNLGKMVVDQCTASDGAPVDRARAWCESIGIPYFRFSPPLSKDIMLDETDDEDLVNMLWDTEVYIYTHR 312
|
|
| PATA |
COG3621 |
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
141-433 |
2.23e-38 |
|
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: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNNQKF--- 217
Cdd:COG3621 9 ILSLDGGGIRGLIPARILAELEERLGKPLAEYFDLIAGTSTGGIIALGLAAGYSAEEILDLYEEEGKEIFPKSRWRKlls 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 218 ------PKHSALGIETCLQEVMGSKTLmSKCTaHRLVVTTAKVTLAPPqlVLFRSYAPRIDskefeqlgyfNPNKILLWK 291
Cdd:COG3621 89 lrglfgPKYDSEGLEKVLKEYFGDTTL-GDLK-TPVLIPSYDLDNGKP--VFFKSPHAKFD----------RDRDFLLVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 292 AIRCTTAAPTYFPSFN---------GMADGALFCNNP--CIMVMTEFAKLKKIENYRgknntdeigcVISVGTGIEP-SY 359
Cdd:COG3621 155 VARATSAAPTYFPPAQiknltgegyALIDGGVFANNPalCALAEALKLLGPDLDDIL----------VLSLGTGTAPrSI 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392899743 360 PINGIDinltsgltgitgNWReIIENTKNLITVFLYqcTSSHNVHvGQSRewcHSMQVPFFRFSPHLAAPFELD 433
Cdd:COG3621 225 PYKKVK------------NWG-ALGWLLPLIDILMD--AQSDAVD-YQLR---QLLGDRYYRLDPELPEEIALD 279
|
|
| Pat_PNPLA8 |
cd07211 |
Patatin-like phospholipase domain containing protein 8; PNPLA8 is a Ca-independent myocardial ... |
141-435 |
2.23e-32 |
|
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: 125.83 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRNRIHWIAGTSCGGIMASSIGV-GIDLADALRLYIIIRKRIFggnNQKFP- 218
Cdd:cd07211 10 ILSIDGGGTRGVVALEILRKIEKLTGKPIHELFDYICGVSTGAILAFLLGLkKMSLDECEELYRKLGKDVF---SQNTYi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 219 -----------KHSALGIETCLQEVMGSKTLMSKC---TAHRLVVTTAKVTLAPPQLVLFRSYA--PRIDSKefeqlgYF 282
Cdd:cd07211 87 sgtsrlvlshaYYDTETWEKILKEMMGSDELIDTSadpNCPKVACVSTQVNRTPLKPYVFRNYNhpPGTRSH------YL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 283 NPNKILLWKAIRCTTAAPTYFPSF----NGMADGALFCNNPCIMVMTEfAKL----KKIEnyrgknntdeigCVISVGTG 354
Cdd:cd07211 161 GSCKHKLWEAIRASSAAPGYFEEFklgnNLHQDGGLLANNPTALALHE-AKLlwpdTPIQ------------CLVSVGTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 355 IEPSYPINGidinltsgltgiTGNWREIIENTKNLItvflYQCTSSHNVHVgqsrewCHSMQVP---FFRFSPHLAAPFE 431
Cdd:cd07211 228 RYPSSVRLE------------TGGYTSLKTKLLNLI----DSATDTERVHT------ALDDLLPpdvYFRFNPVMSECVE 285
|
....
gi 392899743 432 LDNC 435
Cdd:cd07211 286 LDET 289
|
|
| Pat17_PNPLA8_PNPLA9_like |
cd07199 |
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
141-446 |
1.33e-29 |
|
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: 116.66 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEP--LRNRIHWIAGTSCGGIMASSIGVG-IDLADALRLYIIIRKRIFGgnnqkf 217
Cdd:cd07199 1 ILSLDGGGIRGIIPAEILAELEKRLGKPsrIADLFDLIAGTSTGGIIALGLALGrYSAEELVELYEELGRKIFP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 218 pkhsalgietclqevmgsktlmskctahRLVVTTakVTLAPPQLVLFRSYapriDSKEFEQlgyfnPNKILLWKAIRCTT 297
Cdd:cd07199 75 ----------------------------RVLVTA--YDLSTGKPVVFSNY----DAEEPDD-----DDDFKLWDVARATS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 298 AAPTYFPSF--------NGMADGALFCNNPCIMVMTEfakLKKIENYRgknntDEIGCVISVGTGIEPSypingidinlt 369
Cdd:cd07199 116 AAPTYFPPAviesggdeGAFVDGGVAANNPALLALAE---ALRLLAPD-----KDDILVLSLGTGTSPS----------- 176
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899743 370 SGLTGITGNWREIIENTKNLITVFLyqCTSSHNVHVGQSREWCHSMQVPFFRFSPHLAAPFELDNCKIEDITNAMFD 446
Cdd:cd07199 177 SSSSKKASRWGGLGWGRPLLDILMD--AQSDGVDQWLDLLFGSLDSKDNYLRINPPLPGPIPALDDASEANLLALDS 251
|
|
| Pat17_PNPLA8_PNPLA9_like1 |
cd07213 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
141-436 |
1.51e-29 |
|
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: 117.39 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILlavER--ELGEPLRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIF-----GGN 213
Cdd:cd07213 4 ILSLDGGGVKGIVQLVLL---KRlaEEFPSFLDQIDLFAGTSAGSLIALGLALGYSPRQVLKLYEEVGLKVFskssaGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 214 --NQKFPkhSALGIETCLQEVMGSKTLmSKCTaHRLVVTTAKVTLAPPQLVlfRSYAPRIdskeFEQLGYFNPNKILLWK 291
Cdd:cd07213 81 agNNQYF--AAGFLKAFAEVFFGDLTL-GDLK-RKVLVPSFQLDSGKDDPN--RRWKPKL----FHNFPGEPDLDELLVD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 292 AIRCTTAAPTYFPSFNGMADGALFCNNPCIMVMTEfaklkkIENYRGKNNT-DEIgCVISVGTGIEPSYpINGIDINLTS 370
Cdd:cd07213 151 VCLRSSAAPTYFPSYQGYVDGGVFANNPSLCAIAQ------AIGEEGLNIDlKDI-VVLSLGTGRPPSY-LDGANGYGDW 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899743 371 GLTgitgNWRE-----IIENTKNLITvflYQCtsshnVHVGQSRewchsmqvpFFRFSPHLAAPFELDNCK 436
Cdd:cd07213 223 GLL----QWLPdlldlFMDAGVDAAD---FQC-----RQLLGER---------YFRLDPVLPANIDLDDNK 272
|
|
| Pat17_PNPLA8_PNPLA9_like3 |
cd07216 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
141-440 |
9.79e-22 |
|
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum.
Pssm-ID: 132855 [Multi-domain] Cd Length: 309 Bit Score: 95.45 E-value: 9.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLR-----VVLQcAIL--LAVERELGEPLR--NRIHWIAGTSCGGIMAssIGVG---IDLADALRLYIIIRKR 208
Cdd:cd07216 3 LLSLDGGGVRglsslLILK-EIMerIDPKEGLDEPPKpcDYFDLIGGTSTGGLIA--IMLGrlrMTVDECIDAYTRLAKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 209 IFGGNNQKFP---KHSALGIETCLQEVMGSKTLM-------------SKCTAHRLVVTTAKVTLAPPqlVLFRSYAPRid 272
Cdd:cd07216 80 IFSRKRLRLIigdLRTGARFDSKKLAEAIKVILKelgndeddlldegEEDGCKVFVCATDKDVTGKA--VRLRSYPSK-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 273 skeFEQLGYFNPnKIllWKAIRCTTAAPTYFPSFN------GMADGALFCNNPCIMVMTEfAKlkkiENYRGknNTDEIG 346
Cdd:cd07216 156 ---DEPSLYKNA-TI--WEAARATSAAPTFFDPVKigpggrTFVDGGLGANNPIREVWSE-AV----SLWEG--LARLVG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 347 CVISVGTGIePSYPINGIDINLTSGLTGItgnwREIIENTKNLITVFLYQCTsshnvhvgQSREWCHsmqvpFFRFS-PH 425
Cdd:cd07216 223 CLVSIGTGT-PSIKSLGRSAEGAGLLKGL----KDLVTDTEAEAKRFSAEHS--------ELDEEGR-----YFRFNvPH 284
|
330
....*....|....*.
gi 392899743 426 LAAPFELD-NCKIEDI 440
Cdd:cd07216 285 GLEDVGLDeYEKMEEI 300
|
|
| CBASS_lipase |
NF041079 |
CBASS cGAMP-activated phospholipase; |
141-353 |
4.31e-19 |
|
CBASS cGAMP-activated phospholipase;
Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 87.94 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNNQ----- 215
Cdd:NF041079 3 ILSLSGGGYRGLYTASVLAELEEQFGRPIADHFDLICGTSIGGILALALALEIPARELVELFEEHGKDIFPKRKWprrll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 216 ---KFPKHSALGIETCLQEVMGSKTLmSKCTaHRLVVTTAKVTLAPPQlvLFRSyaPRidSKEFEQlgyfnPNKILLWKA 292
Cdd:NF041079 83 gllKKPKYSSEPLREVLEEIFGDKTI-GDLK-HRVLIPAVNYTTGKPQ--VFKT--PH--HPDFTR-----DHKLKLVDV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899743 293 IRCTTAAPTYFP--SFNG--MADGALFCNNPCIMVMTE---FAKlKKIENYRgknntdeigcVISVGT 353
Cdd:NF041079 150 ALATSAAPTYFPlhEFDNeqFVDGGLVANNPGLLGLHEalhFLG-VPYDDVR----------ILSIGT 206
|
|
| Pat17_PNPLA8_PNPLA9_like4 |
cd07217 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
139-357 |
1.48e-16 |
|
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: 81.00 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 139 KVILSLDGGGLRVVLQCAILLAVE----RELGEP---LRNRIHWIAGTSCGGIMASSIGVGIDLADALRLYII------- 204
Cdd:cd07217 1 KKILALDGGGIRGLLSVEILGRIEkdlrTHLDDPefrLGDYFDFVGGTSTGSIIAACIALGMSVTDLLSFYTLngvnmfd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 205 ---IRKRIFGG--NNQKFPKhsalGIETCLQEVMGSKTLMSKCTAHRLVVTTAKVTLAPPQLVlfrSYAPRidSKEFEQL 279
Cdd:cd07217 81 kawLAQRLFLNklYNQYDPT----NLGKKLNTVFPETTLGDDTLRTLLMIVTRNATTGSPWPV---CNNPE--AKYNDSD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 280 GYFNPNKILLWKAIRCTTAAPTYFP----------SFNGMADGALFCNNPCI-MVMTEFAKLKKIeNYR-GKNNTdeigC 347
Cdd:cd07217 152 RSDCNLDLPLWQLVRASTAAPTFFPpevvsiapgtAFVFVDGGVTTYNNPAFqAFLMATAKPYKL-NWEvGADNL----L 226
|
250
....*....|
gi 392899743 348 VISVGTGIEP 357
Cdd:cd07217 227 LVSVGTGFAP 236
|
|
| Pat17_PNPLA8_PNPLA9_like2 |
cd07215 |
Patatin-like phospholipase of bacteria; Patatin is a storage protein of the potato tuber that ... |
141-354 |
1.70e-15 |
|
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: 77.45 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEPLRN---RI----HWIAGTSCGGIMAS-------SIGVGIDLADALRLYI--- 203
Cdd:cd07215 2 ILSIDGGGIRGIIPATILVSVEEKLQKKTGNpeaRLadyfDLVAGTSTGGILTClylcpneSGRPKFSAKEALNFYLerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 204 --IIRKRIFggNNQKF------PKHSALGIETCLQEVMGSKT---LMSKCtahrlVVTTAKVTLAPPqlVLFRSYAPRID 272
Cdd:cd07215 82 nyIFKKKIW--NKIKSrggflnEKYSHKPLEEVLLEYFGDTKlseLLKPC-----LITSYDIERRSP--HFFKSHTAIKN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 273 skefEQLGYfnpnkiLLWKAIRCTTAAPTYFP-----SFNG----MADGALFCNNPCIMVMTEFAKLKkiENYRGKNNTD 343
Cdd:cd07215 153 ----EQRDF------YVRDVARATSAAPTYFEparihSLTGekytLIDGGVFANNPTLCAYAEARKLK--FEQPGKPTAK 220
|
250
....*....|.
gi 392899743 344 EIGCViSVGTG 354
Cdd:cd07215 221 DMIIL-SLGTG 230
|
|
| Patatin |
pfam01734 |
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
142-319 |
1.85e-13 |
|
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: 68.79 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 142 LSLDGGGLRVVLQCAILLAVERELGEPLRnrihwIAGTSCGGIMASSIGVGIDLADALRLYIIIRKRIFGGNNQKFPKHS 221
Cdd:pfam01734 1 LVLSGGGARGAYHLGVLKALGEAGIRFDV-----ISGTSAGAINAALLALGRDPEEIEDLLLELDLNLFLSLIRKRALSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 222 ALGIETC---------------LQEVMGSKTLMSKCTAHRLVVTTAKVTLAPPQLVLFRSYAPRIDSKEFEqlgyfnpNK 286
Cdd:pfam01734 76 LALLRGLigegglfdgdalrelLRKLLGDLTLEELAARLSLLLVVALRALLTVISTALGTRARILLPDDLD-------DD 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 392899743 287 ILLWKAIRCTTAAPTYFP--SFNG--MADGALFCNNP 319
Cdd:pfam01734 149 EDLADAVLASSALPGVFPpvRLDGelYVDGGLVDNVP 185
|
|
| Pat17_isozyme_like |
cd07214 |
Patatin-like phospholipase of plants; Pat17 is an isozyme of patatin cloned from Solanum ... |
141-354 |
3.31e-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: 64.77 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 141 ILSLDGGGLRVVLQCAILLAVERELGEpLRN---RI----HWIAGTSCGGIMASSIGVG-------IDLADALRLYIIIR 206
Cdd:cd07214 6 VLSIDGGGIRGIIPATILEFLEGKLQE-LDGpdaRIadyfDVIAGTSTGGLITAMLTAPnenkrplFAAKDIVQFYLENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 207 KRIF---GGNNQKF---------PKHSALGIETCLQEVMGSKTLMSKCTahRLVVTTAKVTLAPPqlVLFRSYAPRIDSK 274
Cdd:cd07214 85 PKIFpqsTGQFEDDrkklrsllgPKYDGVYLHDLLNELLGDTRLSDTLT--NVVIPTFDIKLLQP--VIFSSSKAKNDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 275 EFEQLGyfnpnkillwKAIRCTTAAPTYFPS--------------FNgMADGALFCNNPCIMVMTEFAKLKKIENYR--G 338
Cdd:cd07214 161 TNARLA----------DVCISTSAAPTYFPAhyfttedsngdireFN-LVDGGVAANNPTLLAISEVTKEIIKDNPFfaS 229
|
250
....*....|....*..
gi 392899743 339 KNNTDEIG-CVISVGTG 354
Cdd:cd07214 230 IKPLDYKKlLVLSLGTG 246
|
|
| Patatin |
cd07198 |
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
142-320 |
1.96e-06 |
|
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 PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.
Pssm-ID: 132837 [Multi-domain] Cd Length: 172 Bit Score: 48.11 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 142 LSLDGGGLRVVLQCAILLAVeRELGEPlrnrIHWIAGTSCGGIMASSIGVGIDLADAlrlYIIIRKRIFGGNNQK---FP 218
Cdd:cd07198 1 LVLSGGGALGIYHVGVAKAL-RERGPL----IDIIAGTSAGAIVAALLASGRDLEEA---LLLLLRLSREVRLRFdgaFP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 219 KHSALGIETCLQEVMGSKTlmskcTAHRLVVTTakvtlappqlvLFRSYAPRIDSKEFEqlgYFNPNKILLWKAIRCTTA 298
Cdd:cd07198 73 PTGRLLGILRQPLLSALPD-----DAHEDASGK-----------LFISLTRLTDGENVL---VSDTSKGELWSAVRASSS 133
|
170 180
....*....|....*....|....*...
gi 392899743 299 APTYF----PSFNGM--ADGALFCNNPC 320
Cdd:cd07198 134 IPGYFgpvpLSFRGRryGDGGLSNNLPV 161
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
9-89 |
6.27e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 41.86 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 9 INAQEIYKRHIdIFHAITYDNIDgLVAAFV-RNEPFDIKDKNGNTPLHLAAKLNR----RLLCravcvyAAGLDLwNSKN 83
Cdd:COG0666 113 VNARDKDGETP-LHLAAYNGNLE-IVKLLLeAGADVNAQDNDGNTPLHLAAANGNleivKLLL------EAGADV-NARD 183
|
....*.
gi 392899743 84 NDGKTP 89
Cdd:COG0666 184 NDGETP 189
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
44-92 |
2.29e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 2.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392899743 44 DIKDKNGNTPLHLAAKLNRRLLCRAVCVYaaGLDlWNSKNNDGKTPIEM 92
Cdd:pfam13857 10 NRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVD-LNLKDEEGLTALDL 55
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
9-92 |
2.29e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 39.94 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 9 INAQEIYKRHIdIFHAITYDNIDgLVAAFV-RNEPFDIKDKNGNTPLHLAAKLNR----RLLCravcvyAAGLDLwNSKN 83
Cdd:COG0666 146 VNAQDNDGNTP-LHLAAANGNLE-IVKLLLeAGADVNARDNDGETPLHLAAENGHleivKLLL------EAGADV-NAKD 216
|
....*....
gi 392899743 84 NDGKTPIEM 92
Cdd:COG0666 217 NDGKTALDL 225
|
|
| Pat_ExoU_VipD_like |
cd07207 |
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ... |
142-319 |
6.49e-03 |
|
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.
Pssm-ID: 132846 Cd Length: 194 Bit Score: 38.03 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 142 LSLDGGGLRVVLQCAILLAVErELGEPLRNrihwIAGTSCGGIMASSIGVGIDLADalrlyiiIRKRIFGGNNQKFPKHS 221
Cdd:cd07207 2 LVFEGGGAKGIAYIGALKALE-EAGILKKR----VAGTSAGAITAALLALGYSAAD-------IKDILKETDFAKLLDSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899743 222 ALGIETcLQEVMGSKTLMSKCTAHRLVV-TTAKVTLAPPQLVLFRSYAPR-----------IDSKEFEQLGYFNPNKILL 289
Cdd:cd07207 70 VGLLFL-LPSLFKEGGLYKGDALEEWLReLLKEKTGNSFATSLLRDLDDDlgkdlkvvatdLTTGALVVFSAETTPDMPV 148
|
170 180 190
....*....|....*....|....*....|....*
gi 392899743 290 WKAIRCTTAAPTYF-PSFNGMA----DGALFCNNP 319
Cdd:cd07207 149 AKAVRASMSIPFVFkPVRLAKGdvyvDGGVLDNYP 183
|
|
| |
