|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
1-389 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 736.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 1 MVTVNEIRQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKEN 80
Cdd:PLN03173 1 MVTVDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 81 PSLCEYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMY 160
Cdd:PLN03173 81 PSVCEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEVEKPLFELV 240
Cdd:PLN03173 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGVEKPLFELV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 241 WTAQTIVPDSEGAIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLK 320
Cdd:PLN03173 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357462733 321 PEKMQATRHVLSEYGNMSSACVLFILDEMRMKSKEDGLATTGEGLEWGVLFGFGPGLTIETVVLRSVST 389
Cdd:PLN03173 321 PEKLRATRHVLSEYGNMSSACVLFILDEMRKKSAEDGLKSTGEGLEWGVLFGFGPGLTVETVVLHSVAP 389
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
16-384 |
4.75e-173 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 486.73 E-value: 4.75e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 16 PATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLT--EEILKENPSlceyMAPSLDA 93
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPE----MSPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 94 RQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRL 173
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 174 AKDLAENNKGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFGDGAAAVIVGSDPLPEV-EKPLFELVWTAQTIVPDSEG 252
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRrERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 253 AIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDY--NSIFWIAHPGGPAILDQVELKLGLKPEKMQATRHV 330
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLGIGLFklAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 357462733 331 LSEYGNMSSACVLFILDEMRMKSKEdglattgEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00831 315 LRRYGNMSSSSVLYVLAYMEAKGRV-------KRGDRGLLIAFGPGFTCESAVW 361
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
4-228 |
4.48e-152 |
|
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.
Pssm-ID: 395142 Cd Length: 225 Bit Score: 428.12 E-value: 4.48e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 4 VNEIRQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKENPSL 83
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 84 CEYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQG 163
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357462733 164 CFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDP 228
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
16-385 |
2.05e-100 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 301.67 E-value: 2.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 16 PATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTelREKFQRMCDKSMIKKRYMHLTEEILKENPSLCEYMAPSLDarq 95
Cdd:COG3424 1 SARILSIATAVPPHRYTQEEIAEFAAELFGLDERD--RRRLRRLFENSGIETRHSVLPLEWYLEPPSFGERNALYIE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 96 dmvvvEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAK 175
Cdd:COG3424 76 -----EALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 176 DLAENNKGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEvekPLFELVWTAQTIVPDSEGAID 255
Cdd:COG3424 151 DFLRADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPG---PGPRILAFRSYLIPDTEDVMG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 256 GHLREAGLTFHLLKDVPGLVSKNIeKALVEAF---QPLNISDYNsiFWIAHPGGPAILDQVELKLGLKPEKMQATRHVLS 332
Cdd:COG3424 227 WDVGDTGFRMVLSPEVPDLIAEHL-APAVEPLlarHGLTIEDID--HWAVHPGGPKVLDAVEEALGLPPEALAHSREVLR 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 357462733 333 EYGNMSSACVLFILDEMRmkskEDGLATTGeglEWGVLFGFGPGLTIETVVLR 385
Cdd:COG3424 304 EYGNMSSATVLFVLERLL----EEGAPAPG---ERGLAMAFGPGFTAELVLLR 349
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
105-385 |
6.92e-17 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 80.51 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTS-GVDMPGADYQLTKLLGLRPyvKRYMMYQQGCFAGGTVLRLAKDLAENNKG 183
Cdd:TIGR00747 54 MGFEAAKRAIENAGISKDDIDLIIVATTTpDHAFPSAACMVQAYLGIKG--IPAFDLSAACAGFIYALSVAKQYIESGKY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 184 ARVLVVCSEITAVTF----RGPSdthldslvgqALFGDGAAAVIVGSDPLPEVEKPL--------FELVWTAQTIVPDSE 251
Cdd:TIGR00747 132 KTVLVVGAEKLSSTLdwtdRGTC----------VLFGDGAGAVVLGESEDPGGIISThlgadgtqGEALYLPAGGRPTSG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 252 GAidGHLREAGltfhllKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLKPEKMQATRHvl 331
Cdd:TIGR00747 202 PS--PFITMEG------NEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVH-- 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 357462733 332 sEYGNMSSACVLFILDEMrmksKEDGLATTGEGLewgVLFGFGPGLTIETVVLR 385
Cdd:TIGR00747 272 -KYGNTSAASIPLALDEL----LRTGRIKPGDLL---LLVAFGGGLTWGAALVR 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
1-389 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 736.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 1 MVTVNEIRQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKEN 80
Cdd:PLN03173 1 MVTVDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 81 PSLCEYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMY 160
Cdd:PLN03173 81 PSVCEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEVEKPLFELV 240
Cdd:PLN03173 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGVEKPLFELV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 241 WTAQTIVPDSEGAIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLK 320
Cdd:PLN03173 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357462733 321 PEKMQATRHVLSEYGNMSSACVLFILDEMRMKSKEDGLATTGEGLEWGVLFGFGPGLTIETVVLRSVST 389
Cdd:PLN03173 321 PEKLRATRHVLSEYGNMSSACVLFILDEMRKKSAEDGLKSTGEGLEWGVLFGFGPGLTVETVVLHSVAP 389
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
1-388 |
0e+00 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 704.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 1 MVTVNEIRQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKEN 80
Cdd:PLN03172 1 APSIAEIRKAQRAEGPATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 81 PSLCEYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMY 160
Cdd:PLN03172 81 PNMCAYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEVEKPLFELV 240
Cdd:PLN03172 161 QQGCFAGGTVLRLAKDLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKIERPLFEIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 241 WTAQTIVPDSEGAIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLK 320
Cdd:PLN03172 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357462733 321 PEKMQATRHVLSEYGNMSSACVLFILDEMRMKSKEDGLATTGEGLEWGVLFGFGPGLTIETVVLRSVS 388
Cdd:PLN03172 321 EEKLRATRHVLSDYGNMSSACVLFILDEMRKKSIEEGKGSTGEGLEWGVLFGFGPGLTVETVVLHSVP 388
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
2-387 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 687.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 2 VTVNEIRQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKENP 81
Cdd:PLN03170 6 VTVEEVRKAQRATGPATVLAIGTATPANCVHQADYPDYYFRITKSEHMTELKEKFKRMCDKSQIRKRYMHLTEEYLAENP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 82 SLCEYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQ 161
Cdd:PLN03170 86 NMCAYMAPSLDARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNRLMMYQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 162 QGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEVEKPLFELVW 241
Cdd:PLN03170 166 QGCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSESHLDSMVGQALFGDGAAAVIVGADPDERVERPLFQLVS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 242 TAQTIVPDSEGAIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLKP 321
Cdd:PLN03170 246 ASQTILPDSEGAIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAKVGLEK 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357462733 322 EKMQATRHVLSEYGNMSSACVLFILDEMRMKSKEDGLATTGEGLEWGVLFGFGPGLTIETVVLRSV 387
Cdd:PLN03170 326 ERMRATRHVLSEYGNMSSACVLFILDEMRKRSAEDGQATTGEGFDWGVLFGFGPGLTVETVVLHSV 391
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
8-389 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 563.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 8 RQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKENPSLCEYM 87
Cdd:PLN03168 7 RGQPRAEGPACVLGIGTAVPPAEFLQSEYPDFFFNITNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVLKANPGICTYM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 88 APSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAG 167
Cdd:PLN03168 87 EPSLNVRHDIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGADHALAKLLGLKPTVKRVMMYQTGCFGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 168 GTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEVEKPLFELVWTAQTIV 247
Cdd:PLN03168 167 ASVLRVAKDLAENNKGARVLAVASEVTAVTYRAPSENHLDGLVGSALFGDGAGVYVVGSDPKPEVEKALFEVHWAGETIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 248 PDSEGAIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLKPEKMQAT 327
Cdd:PLN03168 247 PESDGAIDGHLTEAGLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQGS 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357462733 328 RHVLSEYGNMSSACVLFILDEMRMKSKEDGLATTGEGLEWGVLFGFGPGLTIETVVLRSVST 389
Cdd:PLN03168 327 RDILSEFGNMSSASVLFVLDQIRQRSVKMGASTLGEGSEFGFFIGFGPGLTLEVLVLRAAAN 388
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
16-384 |
4.75e-173 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 486.73 E-value: 4.75e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 16 PATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLT--EEILKENPSlceyMAPSLDA 93
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPE----MSPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 94 RQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRL 173
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 174 AKDLAENNKGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFGDGAAAVIVGSDPLPEV-EKPLFELVWTAQTIVPDSEG 252
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRrERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 253 AIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDY--NSIFWIAHPGGPAILDQVELKLGLKPEKMQATRHV 330
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLGIGLFklAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 357462733 331 LSEYGNMSSACVLFILDEMRMKSKEdglattgEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00831 315 LRRYGNMSSSSVLYVLAYMEAKGRV-------KRGDRGLLIAFGPGFTCESAVW 361
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
4-389 |
2.46e-172 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 486.43 E-value: 2.46e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 4 VNEIRQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKENPSL 83
Cdd:PLN03171 10 LGEICRAQRADGLAAVLAIGTANPANCVPQDEFPDFYFRATKSDHLTALKDKFKRICQELGVQKRYLHHTEELLSAHPEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 84 CEYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQG 163
Cdd:PLN03171 90 LDHDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAHIPGVDFRLVPLLGLRPSVRRTMLHLNG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 164 CFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDPLpEVEKPLFELVWTA 243
Cdd:PLN03171 170 CFAGAAALRLAKDLAENNRGARVLVVAAEITLLLFNGPDEGCFQTLLNQGLFGDGAAAVIVGADAD-AAERPLFEIVSAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 244 QTIVPDSEGAIDGHLREAGLTFHL-LKDVPGLVSKNIEKALVEAFQPLNISD----YNSIFWIAHPGGPAILDQVELKLG 318
Cdd:PLN03171 249 QAIIPESDDAINMHFTEGGLDGNIgTRQVPGLIGDNIERCLLDAFAPLLGGDggaeWNDLFWAVHPGSSAILDQVDAALG 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357462733 319 LKPEKMQATRHVLSEYGNMSSACVLFILDEMRMKSKEDglATTGEGLEWGVLFGFGPGLTIETVVLRSVST 389
Cdd:PLN03171 329 LEPEKLAASRRVLSDYGNMFGATVIFALDELRRQMEEA--AAAGAWPELGVMMAFGPGLTVDAMLLHASGH 397
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
4-228 |
4.48e-152 |
|
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.
Pssm-ID: 395142 Cd Length: 225 Bit Score: 428.12 E-value: 4.48e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 4 VNEIRQAQRAEGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTELREKFQRMCDKSMIKKRYMHLTEEILKENPSL 83
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 84 CEYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQG 163
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357462733 164 CFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDP 228
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
8-387 |
9.16e-133 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 385.59 E-value: 9.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 8 RQAQRaeGPATVFAIGTANPQNCVDQSTYPDFYFRITNSEhKTELREKFQRMCDKSMIKKRYMHLTEEILKENPSLCEYM 87
Cdd:PLN03169 15 RAANP--GKATILALGKAFPSQLVPQEYLVDGYFRDTKCD-DPALKEKLERLCKTTTVKTRYVVMSKEILDKYPELATEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 88 APSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAG 167
Cdd:PLN03169 92 TPTIKQRLDIANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEARLPGGDLYLAKQLGLSPDVQRVMLYFLGCSGG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 168 GTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEVEKPLFELVWTAQTIV 247
Cdd:PLN03169 172 VAGLRVAKDIAENNPGSRVLLTTSETTILGFRPPSPDRPYDLVGAALFGDGAAAVIIGADPIPVSESPFFELHTAIQQFL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 248 PDSEGAIDGHLREAGLTFHLLKDVPGLVSKNIE----KALVEAfqPLNISDYNSIFWIAHPGGPAILDQVELKLGLKPEK 323
Cdd:PLN03169 252 PGTEKTIDGRLTEEGINFKLGRELPQKIEDNIEgfckKLMKKA--GLVEKDYNDLFWAVHPGGPAILNRLEKKLKLAPEK 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357462733 324 MQATRHVLSEYGNMSSACVLFILDEMRMKSKEDGlattGEGLEWGVLFGFGPGLTIETVVLRSV 387
Cdd:PLN03169 330 LECSRRALMDYGNVSSNTIVYVLEYMREELKKKG----EEDEEWGLILAFGPGITFEGILARNL 389
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
16-385 |
2.05e-100 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 301.67 E-value: 2.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 16 PATVFAIGTANPQNCVDQSTYPDFYFRITNSEHKTelREKFQRMCDKSMIKKRYMHLTEEILKENPSLCEYMAPSLDarq 95
Cdd:COG3424 1 SARILSIATAVPPHRYTQEEIAEFAAELFGLDERD--RRRLRRLFENSGIETRHSVLPLEWYLEPPSFGERNALYIE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 96 dmvvvEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAK 175
Cdd:COG3424 76 -----EALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 176 DLAENNKGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFGDGAAAVIVGSDPLPEvekPLFELVWTAQTIVPDSEGAID 255
Cdd:COG3424 151 DFLRADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPG---PGPRILAFRSYLIPDTEDVMG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 256 GHLREAGLTFHLLKDVPGLVSKNIeKALVEAF---QPLNISDYNsiFWIAHPGGPAILDQVELKLGLKPEKMQATRHVLS 332
Cdd:COG3424 227 WDVGDTGFRMVLSPEVPDLIAEHL-APAVEPLlarHGLTIEDID--HWAVHPGGPKVLDAVEEALGLPPEALAHSREVLR 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 357462733 333 EYGNMSSACVLFILDEMRmkskEDGLATTGeglEWGVLFGFGPGLTIETVVLR 385
Cdd:COG3424 304 EYGNMSSATVLFVLERLL----EEGAPAPG---ERGLAMAFGPGFTAELVLLR 349
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
238-387 |
1.93e-87 |
|
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in the N-terminal domain.
Pssm-ID: 397089 Cd Length: 151 Bit Score: 261.23 E-value: 1.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 238 ELVWTAQTIVPDSEGAIDGHLREAGLTFHLLKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKL 317
Cdd:pfam02797 1 ELVSAAQTFLPNTDGVIDGHLTEEGLTFHLGRDVPQKIEENIEEFLKKAFEPLGISEWNSLFWIVHPGGPAILDRVETKL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 318 GLKPEKMQATRHVLSEYGNMSSACVLFILDEMRMKSKEDGLATTGEGLEWGVLFGFGPGLTIETVVLRSV 387
Cdd:pfam02797 81 GLEPEKLEASRRALMDYGNVSSATVLFILDEMRKKSLKKGLATTGEGLDWGVLLAFGPGLTFETVVLRSV 150
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
102-384 |
7.66e-60 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 194.20 E-value: 7.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 102 VPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVD-MPGADYQLTKLLGLrPYVKRYMMYQqGCFAGGTVLRLAKDLAEN 180
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGeFSGAAGQLAYHLGI-SGGPAYSVNQ-ACATGLTALALAVQQVQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 181 NKGARVLVVCSEItavtfrgpsdthldslvgqALFGDGAAAVIVGSDP--LPEVEKPLFELVWTAQTIVPDSEgaidghl 258
Cdd:cd00327 85 GKADIVLAGGSEE-------------------FVFGDGAAAAVVESEEhaLRRGAHPQAEIVSTAATFDGASM------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 259 reagltfhllkdVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLKPEKMQ--ATRHVLSEYGN 336
Cdd:cd00327 139 ------------VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRspAVSATLIMTGH 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 357462733 337 MSSACVLFILDEMRMKSKEDGLATTGEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00327 207 PLGAAGLAILDELLLMLEHEFIPPTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
102-384 |
5.20e-57 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 189.38 E-value: 5.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 102 VPKLGKEAATKAIKEWG----QPKSKITHLIFCTTSGVD----------------------MPGADYQLTKLLGLRpyVK 155
Cdd:cd00825 11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgadamravgpyvvtkamFPGASGQIATPLGIH--GP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 156 RYMMYQqGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDT------------HLDSLVGQALFGDGAAAVI 223
Cdd:cd00825 89 AYDVSA-ACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAmgalstpekasrTFDAAADGFVFGDGAGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 224 VGSDP--LPEVEKPLFELVWTAQTIVPDSEGAidghlreagltfhllkdvPGLVSKNIEKALVEAFQPLNISDYNSIFWI 301
Cdd:cd00825 168 VEELEhaLARGAHIYAEIVGTAATIDGAGMGA------------------FAPSAEGLARAAKEALAVAGLTVWDIDYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 302 AHPGGPAILDQVELKLGLKPEKMQ--ATRHVLSEYGNMSSACVLFILDEMRMKSKEDGLA------------------TT 361
Cdd:cd00825 230 AHGTGTPIGDVKELKLLRSEFGDKspAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPpsihieeldeaglnivteTT 309
|
330 340
....*....|....*....|...
gi 357462733 362 GEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00825 310 PRELRTALLNGFGLGGTNATLVL 332
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
21-384 |
9.95e-41 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 146.42 E-value: 9.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 21 AIGTANPQNCVDQSTYPDFYFRITNSEHKtelrekfqrmcdksMIKKRYMHLTEEIlkeNPSLCEymapsldarqdmvvv 100
Cdd:cd00827 6 AIGAYLPRYRVDNEELAEGLGVDPGKYTT--------------GIGQRHMAGDDED---VPTMAV--------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 101 evpklgkEAATKAIKEWGQPKSKITHLIFCTTSGVD-MPGADYQLTKLLGLRPyVKRYMMyQQGCFAGGTVLRLAKDLAE 179
Cdd:cd00827 54 -------EAARRALERAGIDPDDIGLLIVATESPIDkGKSAATYLAELLGLTN-AEAFDL-KQACYGGTAALQLAANLVE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 180 NNKGARVLVVCSEItavtFRGPSDTHLDslvGQALFGDGAAAVIVGSDPlpevEKPLFELVWTAQTI----VPDSEGAID 255
Cdd:cd00827 125 SGPWRYALVVASDI----ASYLLDEGSA---LEPTLGDGAAAMLVSRNP----GILAAGIVSTHSTSdpgyDFSPYPVMD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 256 GHLREAGLTFHLL--------KDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLKPEKMQAT 327
Cdd:cd00827 194 GGYPKPCKLAYAIrltaepagRAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLGGPPEKASQT 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 357462733 328 RH-VLSEYGNMSSACVLFILDEMRMKSKEDGlattGEGLewgVLFGFGPGLTIETVVL 384
Cdd:cd00827 274 RWiLLRRVGNMYAASILLGLASLLESGKLKA----GDRV---LLFSYGSGFTAEAFVL 324
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
105-385 |
6.92e-17 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 80.51 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTS-GVDMPGADYQLTKLLGLRPyvKRYMMYQQGCFAGGTVLRLAKDLAENNKG 183
Cdd:TIGR00747 54 MGFEAAKRAIENAGISKDDIDLIIVATTTpDHAFPSAACMVQAYLGIKG--IPAFDLSAACAGFIYALSVAKQYIESGKY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 184 ARVLVVCSEITAVTF----RGPSdthldslvgqALFGDGAAAVIVGSDPLPEVEKPL--------FELVWTAQTIVPDSE 251
Cdd:TIGR00747 132 KTVLVVGAEKLSSTLdwtdRGTC----------VLFGDGAGAVVLGESEDPGGIISThlgadgtqGEALYLPAGGRPTSG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 252 GAidGHLREAGltfhllKDVPGLVSKNIEKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVELKLGLKPEKMQATRHvl 331
Cdd:TIGR00747 202 PS--PFITMEG------NEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVH-- 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 357462733 332 sEYGNMSSACVLFILDEMrmksKEDGLATTGEGLewgVLFGFGPGLTIETVVLR 385
Cdd:TIGR00747 272 -KYGNTSAASIPLALDEL----LRTGRIKPGDLL---LLVAFGGGLTWGAALVR 317
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
105-384 |
7.47e-17 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTSGVD-MPGADYQLTKLLGLrpyvKRYMMY--QQGC--FAGGtvLRLAKDLAE 179
Cdd:cd00830 53 LAVEAAKKALEDAGIDADDIDLIIVATSTPDYlFPATACLVQARLGA----KNAAAFdiNAACsgFLYG--LSTAAGLIR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 180 NNKGARVLVVCSEITA--VTFRGPSdTHLdslvgqaLFGDGAAAVIVGSDPlpevEKP------------LFELVWT--- 242
Cdd:cd00830 127 SGGAKNVLVVGAETLSriLDWTDRS-TAV-------LFGDGAGAVVLEATE----EDPgildsvlgsdgsGADLLTIpag 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 243 AQTIVPDSEGAIDGHLREAG--LTFHLLKDVPGLVSKNIEKALVeafQPLNIsDYnsiFWIaHPGGPAILDQVELKLGLK 320
Cdd:cd00830 195 GSRSPFEDAEGGDPYLVMDGreVFKFAVRLMPESIEEALEKAGL---TPDDI-DW---FVP-HQANLRIIEAVAKRLGLP 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357462733 321 PEKMQatrHVLSEYGNMSSACVLFILDEMRmkskEDGLATTGEGLewgVLFGFGPGLTIETVVL 384
Cdd:cd00830 267 EEKVV---VNLDRYGNTSAASIPLALDEAI----EEGKLKKGDLV---LLLGFGAGLTWGAALL 320
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
105-228 |
2.94e-14 |
|
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 442651 [Multi-domain] Cd Length: 382 Bit Score: 73.29 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTSGVDM--PGADYqLTKLLGLRPYVkRYMMYQQGCFAGGTVLRLAKDLAENNK 182
Cdd:COG3425 54 MAANAARRALDRAGIDPSDIGAVYVGTESGPDAskPIATY-VHGALGLPPNC-RAFELKFACYAGTAALQAALGWVASGP 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 357462733 183 GARVLVVCSEItavtfrgpSDTHLDSlVGQALFGDGAAAVIVGSDP 228
Cdd:COG3425 132 NKKALVIASDI--------ARYGPGS-AGEYTQGAGAVAMLVGADP 168
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
105-385 |
1.45e-13 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 70.91 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTSGvDM--PGADYQLTKLLGLRpyvkrymmyqqGCFA-------GGTV--LRL 173
Cdd:COG0332 54 LAVEAARKALEAAGIDPEDIDLIIVATVTP-DYlfPSTACLVQHKLGAK-----------NAAAfdinaacSGFVyaLSV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 174 AKDLAENNKGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFGDGAAAVIVGSDplpEVEKPLFELVWTAqtivpDSEG 252
Cdd:COG0332 122 AAALIRSGQAKNVLVVGAETlSRIVDWTDRSTCV-------LFGDGAGAVVLEAS---EEGPGILGSVLGS-----DGSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 253 A----IDG-----HLREAGLTFHLL----KDVPGLVSKNIEKALVEAFQPLNISdYNSIFWIA-HPGGPAILDQVELKLG 318
Cdd:COG0332 187 AdllvVPAggsrnPPSPVDEGDHYLrmdgREVFKFAVRNLPEVIREALEKAGLT-LDDIDWFIpHQANLRIIEAVAKRLG 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357462733 319 LKPEKMQATrhvLSEYGNMSSACVLFILDEMRmkskEDGLATTGEGLewgVLFGFGPGLTIETVVLR 385
Cdd:COG0332 266 LPEEKVVVN---IDRYGNTSAASIPLALDEAL----REGRIKPGDLV---LLAGFGAGLTWGAAVLR 322
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
301-385 |
8.39e-09 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 52.12 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 301 IAHPGGPAILDQVELKLGLKPEKMQATrhvLSEYGNMSSACVLFILDEMRmkskEDGLATTGEGLewgVLFGFGPGLTIE 380
Cdd:pfam08541 15 VPHQANLRIIDAVAKRLGLPPEKVVVN---LDEYGNTSAASIPLALDEAV----EEGKLKPGDLV---LLVGFGAGLTWG 84
|
....*
gi 357462733 381 TVVLR 385
Cdd:pfam08541 85 AALLR 89
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
150-374 |
4.99e-08 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 54.58 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 150 LRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLdsLVGQALFGDGAAAVIVgSDPL 229
Cdd:PLN02854 236 LRTDIKSYNLGGMGCSAGLISIDLANDLLKANPNSYAVVVSTENITLNWYFGNDRSM--LLCNCIFRMGGAAVLL-SNKA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 230 PEVEKPLFELVWTAQTivpdSEGAIDGHLR----------EAGLTF-HLLKDVPG------------------------- 273
Cdd:PLN02854 313 RDRKRSKYQLVHTVRT----HKGADDKNYNcvyqreddkgTIGVSLaRELMAVAGdalktnittlgplvlplseqfmffv 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 274 -LVSKNIEKALVEAFQPlnisDYNSIF--WIAHPGGPAILDQVELKLGLKPEKMQATRHVLSEYGNMSSACVLFILDEMR 350
Cdd:PLN02854 389 tLVRRKLLKAKVKPYIP----DFKLAFehFCIHAGGRAVLDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWYELAYTE 464
|
250 260
....*....|....*....|....
gi 357462733 351 MKskedGLATTGEGLeWGVLFGFG 374
Cdd:PLN02854 465 AK----GRVSAGDRV-WQIAFGSG 483
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
150-389 |
1.23e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 53.54 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 150 LRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-ITAVTFRGpSDTHLdsLVGQALFGDGAAAVIVGSDP 228
Cdd:PLN00415 182 LKTDVKTYNLSGMGCSAGAISVDLATNLLKANPNTYAVIVSTEnMTLSMYRG-NDRSM--LVPNCLFRVGGAAVMLSNRS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 229 LPEVeKPLFELVwtaqTIVPDSEGAIDGHLREAgltfHLLKDVPGLVSKNIEKAL-----------VEAFQPL------- 290
Cdd:PLN00415 259 QDRV-RSKYELT----HIVRTHKGSSDKHYTCA----EQKEDSKGIVGVALSKELtvvagdtlktnLTALGPLvlplsek 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 291 ---------------NISDYNSIF------WIAHPGGPAILDQVELKLGLKPEKMQATRHVLSEYGNMSSACVLFILDEM 349
Cdd:PLN00415 330 lrfilflvksklfrlKVSPYVPDFklcfkhFCIHAGGRALLDAVEKGLGLSEFDLEPSRMTLHRFGNTSSSSLWYELAYV 409
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 357462733 350 RMKSKedglATTGEGLeWGVlfGFGPGLTIETVVLRSVST 389
Cdd:PLN00415 410 EAKCR----VKRGDRV-WQL--AFGSGFKCNSIVWRALRT 442
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
105-385 |
1.63e-07 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 52.38 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTSGVD-MPGADYQLTKLLGLRpyvkrymmyqqGCFA-------GGTV--LRLA 174
Cdd:PRK09352 55 LATEAAKKALEAAGIDPEDIDLIIVATTTPDYaFPSTACLVQARLGAK-----------NAAAfdlsaacSGFVyaLSTA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 175 KDLAENNKGARVLVVCSEI-----------TAVtfrgpsdthldslvgqaLFGDGAAAVIVGSDplpevekplfelvwta 243
Cdd:PRK09352 124 DQFIRSGAYKNVLVIGAEKlsrivdwtdrsTCV-----------------LFGDGAGAVVLGAS---------------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 244 qtivpDSEGAIDGHLREAGLTFHLLKdVPGLVS---------------------KNIEKALVEAFQ--PLNISDynsIFW 300
Cdd:PRK09352 171 -----EEPGILSTHLGSDGSYGDLLY-LPGGGSrgpaspgylrmegrevfkfavRELAKVAREALEaaGLTPED---IDW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 301 -IAHPGGPAILDQVELKLGLKPEKMQATrhvLSEYGNMSSACVLFILDEMrmksKEDGLATTGEGLewgVLFGFGPGLTI 379
Cdd:PRK09352 242 lVPHQANLRIIDATAKKLGLPMEKVVVT---VDKYGNTSAASIPLALDEA----VRDGRIKRGDLV---LLEGFGGGLTW 311
|
....*.
gi 357462733 380 ETVVLR 385
Cdd:PRK09352 312 GAALVR 317
|
|
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
150-374 |
1.95e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 52.71 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 150 LRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-ITAVTFRGPSDThldSLVGQALFGDGAAAVIVgSDP 228
Cdd:PLN02377 220 LRGNIRSFNLGGMGCSAGVIAVDLAKDMLQVHRNTYAVVVSTEnITQNWYFGNKKS---MLIPNCLFRVGGSAVLL-SNK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 229 LPEVEKPLFELVWTAQTivpdSEGAIDGHLR-------EAGLT-FHLLKDVPGLVSKNIeKALVEAFQPL---------- 290
Cdd:PLN02377 296 SRDKRRSKYKLVHVVRT----HRGADDKAFRcvyqeqdDAGKTgVSLSKDLMAIAGEAL-KTNITTLGPLvlpiseqllf 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 291 ----------------NISDYNSIF--WIAHPGGPAILDQVELKLGLKPEKMQATRHVLSEYGNMSSACVLFILDEMRMK 352
Cdd:PLN02377 371 fatlvvkklfnkkmkpYIPDFKLAFdhFCIHAGGRAVIDELEKNLQLLPVHVEASRMTLHRFGNTSSSSIWYELAYIEAK 450
|
250 260
....*....|....*....|..
gi 357462733 353 SKedglATTGEGLeWGVLFGFG 374
Cdd:PLN02377 451 GR----MRKGNRV-WQIAFGSG 467
|
|
| PLN02932 |
PLN02932 |
3-ketoacyl-CoA synthase |
150-374 |
2.89e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 178520 Cd Length: 478 Bit Score: 52.34 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 150 LRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-ITAVTFRGPSDThldSLVGQALFGDGAAAVIVgSDP 228
Cdd:PLN02932 196 LRDNIKSLNLGGMGCSAGVIAIDAAKSLLQVHRNTYALVVSTEnITQNLYLGNNKS---MLVTNCLFRIGGAAILL-SNR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 229 LPEVEKPLFELVWTAQTIVPDSEGAIDGHLRE------AGLTfhLLKDVPgLVSKNIEKALVEAFQPL------------ 290
Cdd:PLN02932 272 SRDRKRAKYELVHTVRVHTGADDRSYECATQEededgiVGVS--LSKNLP-MVAARTLKINIATLGPLvlplsekfhffv 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 291 ----------NISDYNSIFWIA------HPGGPAILDQVELKLGLKPEKMQATRHVLSEYGNMSSACVLFILDEMRMKsk 354
Cdd:PLN02932 349 rfvkkkffnpKLKHYIPDFKLAfehfciHAGGRALIDEMEKNLHLTPLDVEASRMTLHRFGNTSSSSIWYELAYTEAK-- 426
|
250 260
....*....|....*....|
gi 357462733 355 edGLATTGEGLeWGVLFGFG 374
Cdd:PLN02932 427 --GRMKKGDRI-WQIALGSG 443
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
105-378 |
8.00e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 50.25 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTSGVDM-PGADYQLTKLLGLRpyvkrymmyQQGCF------AGGTV-LRLAKD 176
Cdd:PRK12879 56 LAIKAAERALARAGLDAEDIDLIIVATTTPDYLfPSTASQVQARLGIP---------NAAAFdinaacAGFLYgLETANG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 177 LAENNKGARVLVVCSE-ITAVTfrgpsD-THLDSLVgqaLFGDGAAAVIVGSDplpEVEKPLFELVWTAqtivpDSEGAI 254
Cdd:PRK12879 127 LITSGLYKKVLVIGAErLSKVT-----DyTDRTTCI---LFGDGAGAVVLEAT---ENEPGFIDYVLGT-----DGDGGD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 255 dgHLREAGL-----------TFHLL-------KDVPGLVSKNIEKALVEAfqPLNISDynsIFW-IAHPGGPAILDQVEL 315
Cdd:PRK12879 191 --ILYRTGLgttmdrdalsgDGYIVqngrevfKWAVRTMPKGARQVLEKA--GLTKDD---IDWvIPHQANLRIIESLCE 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357462733 316 KLGLKPEKmqaTRHVLSEYGNMSSACVLFILDEMRmkskEDGLATTGEGLewgVLFGFGPGLT 378
Cdd:PRK12879 264 KLGIPMEK---TLVSVEYYGNTSAATIPLALDLAL----EQGKIKPGDTL---LLYGFGAGLT 316
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
17-385 |
4.25e-06 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 48.02 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 17 ATVFAIGTANPQNCVDQSTYPDFyfrITNSEHKTELRekfqrmcdkSMIKKRYMhlteeilkenpslceymAPSLDArqd 96
Cdd:CHL00203 3 VHILSTGSSVPNFSVENQQFEDI---IETSDHWISTR---------TGIKKRHL-----------------APSSTS--- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 97 mvvveVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGlrpyVKRYMMYQQGCFAGGTVLRL--A 174
Cdd:CHL00203 51 -----LTKLAAEAANKALDKAHMDPLEIDLIILATSTPDDLFGSASQLQAEIG----ATRAVAFDITAACSGFILALvtA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 175 KDLAENNKGARVLVVcseitavtfrgPSDTHLDSLVGQ-----ALFGDGAAAVIVGSDPLPEVEKplFELvwtaqtivpD 249
Cdd:CHL00203 122 TQFIQNGSYKNILVV-----------GADTLSKWIDWSdrktcILFGDGAGAAIIGASYENSILG--FKL---------C 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 250 SEGAIDGHLR---------EAGLT--FHLLKDVPGLVSKNIEK--------ALVEAFQPLNISDYNSIFWIAHPGGPAIL 310
Cdd:CHL00203 180 TDGKLNSHLQlmnkpvnnqSFGTTklPQGQYQSISMNGKEVYKfavfqvpaVIIKCLNALNISIDEVDWFILHQANKRIL 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357462733 311 DQVELKLGLKPEKMQATrhvLSEYGNMSSACVLFILDEMRMKSKedglATTGEGLewgVLFGFGPGLTIETVVLR 385
Cdd:CHL00203 260 EAIANRLSVPNSKMITN---LEKYGNTSAASIPLALDEAIQNNK----IQPGQII---VLSGFGAGLTWGAIVLK 324
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
105-385 |
5.22e-06 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 48.19 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 105 LGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGlrpyVKRYMMYQQGCFAGGTVLRL--AKDLAENNK 182
Cdd:PLN02326 99 LAVEAAKKALEMAGVDPEDVDLVLLCTSSPDDLFGSAPQVQAALG----CTNALAFDLTAACSGFVLGLvtAARFIRGGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 183 GARVLVV----CSEITAVTFRGPSdthldslvgqALFGDGAAAVIVGSDPLPEV-------------EKPLFELVWTAQT 245
Cdd:PLN02326 175 YKNVLVIgadaLSRYVDWTDRGTC----------ILFGDGAGAVVLQACDDDEDgllgfdmhsdgngHKHLHATFKGEDD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 246 IVPDSEGAIDGHLREAGLTFHLL----KDVPGL----VSKNIEKALVEAFQPLNisdynSIFW-IAHPGGPAILDQVELK 316
Cdd:PLN02326 245 DSSGGNTNGVGDFPPKKASYSCIqmngKEVFKFavrcVPQVIESALQKAGLTAE-----SIDWlLLHQANQRIIDAVAQR 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357462733 317 LGLKPEKMQATrhvLSEYGNMSSACVLFILDEM----RMKsKEDGLATTgeglewgvlfGFGPGLTIETVVLR 385
Cdd:PLN02326 320 LGIPPEKVISN---LANYGNTSAASIPLALDEAvrsgKVK-KGDVIATA----------GFGAGLTWGSAIVR 378
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
150-389 |
7.23e-06 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 48.05 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 150 LRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLdsLVGQALFGDGAAAVIVgSDPL 229
Cdd:PLN02192 224 LRGNILSYNLGGMGCSAGLISIDLAKHLLQVHPNSYALVISMENITLNWYFGNDRSM--LVSNCLFRMGGAAILL-SNKR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 230 PEVEKPLFELVWTAQT-------------IVPDSEGAIDGHLRE-----AGLTFHLLKDVPG---------------LVS 276
Cdd:PLN02192 301 SDRRRSKYQLVHTVRThkgaddkcfacvtQEEDSAGKIGVSLSKdlmavAGDALKTNITTLGplvlpmseqllffatLVG 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 277 KNIEKALVEAFQPlnisDYNSIF--WIAHPGGPAILDQVELKLGLKPEKMQATRHVLSEYGNMSSACVLFILdemrMKSK 354
Cdd:PLN02192 381 KKLFKMKLKPYIP----DFKLAFehFCIHAGGRAVLDELEKNLQLSDWHMEPSRMTLYRFGNTSSSSLWYEL----AYSE 452
|
250 260 270
....*....|....*....|....*....|....*
gi 357462733 355 EDGLATTGEGLeWGVlfGFGPGLTIETVVLRSVST 389
Cdd:PLN02192 453 AKGRIKKGDRT-WQI--AFGSGFKCNSAVWKALRT 484
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
149-272 |
1.27e-05 |
|
FAE1/Type III polyketide synthase-like protein; The members of this family are described as 3-ketoacyl-CoA synthases, type III polyketide synthases, fatty acid elongases and fatty acid condensing enzymes, and are found in both prokaryotic and eukaryotic (mainly plant) species. The region featured in this family contains the active site residues, as well as motifs involved in substrate binding.
Pssm-ID: 429970 Cd Length: 290 Bit Score: 46.47 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 149 GLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-ITAVTFRGpSDTHLdsLVGQALFGDGAAAVIVGSD 227
Cdd:pfam08392 130 KLRSDIKSYNLSGMGCSAGLISIDLAKNLLQVHPNTYALVVSTEnITPNWYFG-NDRSM--LLPNCLFRMGGAAVLLSNR 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 357462733 228 PLpEVEKPLFELVWTAQTIVpdseGAIDGHLR-------EAGLT-FHLLKDVP 272
Cdd:pfam08392 207 PA-DRRRAKYELVHTVRTHK----GADDRAYNcvyqeedEDGKVgVSLSKDLM 254
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
161-228 |
2.07e-05 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 42.50 E-value: 2.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357462733 161 QQGCfAGGTV-LRLAKDLAENNKGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFGDGAAAVIVGSDP 228
Cdd:pfam08545 4 NAAC-SGFVYaLSTAAALIRSGRAKNVLVIGAETlSKILDWTDRSTAV-------LFGDGAGAVVLEATD 65
|
|
| |
