|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
6-388 |
0e+00 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 707.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 6 MPSLDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKEN 85
Cdd:PLN03172 1 APSIAEIRKAQRAEGPATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 86 PNMCAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMY 165
Cdd:PLN03172 81 PNMCAYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 166 QQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEM 245
Cdd:PLN03172 161 QQGCFAGGTVLRLAKDLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKI-ERPLFEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 246 VSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKLGL 325
Cdd:PLN03172 240 VSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 99923763 326 KEEKMRATRHVMREYGNMSSACVLFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETV 388
Cdd:PLN03172 320 KEEKLRATRHVLSDYGNMSSACVLFILDEMRKKSIEEGKGSTGEGLEWGVLFGFGPGLTVETV 382
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
8-388 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 698.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 8 SLDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPN 87
Cdd:PLN03170 7 TVEEVRKAQRATGPATVLAIGTATPANCVHQADYPDYYFRITKSEHMTELKEKFKRMCDKSQIRKRYMHLTEEYLAENPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 88 MCAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQ 167
Cdd:PLN03170 87 MCAYMAPSLDARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNRLMMYQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 168 GCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEMVS 247
Cdd:PLN03170 167 GCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSESHLDSMVGQALFGDGAAAVIVGADPDERV-ERPLFQLVS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 248 AAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKLGLKE 327
Cdd:PLN03170 246 ASQTILPDSEGAIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAKVGLEK 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 99923763 328 EKMRATRHVMREYGNMSSACVLFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETV 388
Cdd:PLN03170 326 ERMRATRHVLSEYGNMSSACVLFILDEMRKRSAEDGQATTGEGFDWGVLFGFGPGLTVETV 386
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
6-388 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 697.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 6 MPSLDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKEN 85
Cdd:PLN03173 1 MVTVDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 86 PNMCAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMY 165
Cdd:PLN03173 81 PSVCEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 166 QQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEM 245
Cdd:PLN03173 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGV-EKPLFEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 246 VSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKLGL 325
Cdd:PLN03173 240 VSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 99923763 326 KEEKMRATRHVMREYGNMSSACVLFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETV 388
Cdd:PLN03173 320 KPEKLRATRHVLSEYGNMSSACVLFILDEMRKKSAEDGLKSTGEGLEWGVLFGFGPGLTVETV 382
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
13-388 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 551.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 13 RKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNMCAYM 92
Cdd:PLN03168 7 RGQPRAEGPACVLGIGTAVPPAEFLQSEYPDFFFNITNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVLKANPGICTYM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 93 APSLDARQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAG 172
Cdd:PLN03168 87 EPSLNVRHDIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGADHALAKLLGLKPTVKRVMMYQTGCFGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 173 GTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEMVSAAQTI 252
Cdd:PLN03168 167 ASVLRVAKDLAENNKGARVLAVASEVTAVTYRAPSENHLDGLVGSALFGDGAGVYVVGSDPKPEV-EKALFEVHWAGETI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 253 LPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKLGLKEEKMRA 332
Cdd:PLN03168 246 LPESDGAIDGHLTEAGLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 99923763 333 TRHVMREYGNMSSACVLFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETV 388
Cdd:PLN03168 326 SRDILSEFGNMSSASVLFVLDQIRQRSVKMGASTLGEGSEFGFFIGFGPGLTLEVL 381
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
8-388 |
5.06e-171 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 482.97 E-value: 5.06e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 8 SLDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPN 87
Cdd:PLN03171 9 NLGEICRAQRADGLAAVLAIGTANPANCVPQDEFPDFYFRATKSDHLTALKDKFKRICQELGVQKRYLHHTEELLSAHPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 88 MCAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQ 167
Cdd:PLN03171 89 FLDHDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAHIPGVDFRLVPLLGLRPSVRRTMLHLN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 168 GCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSvgEKPIFEMVS 247
Cdd:PLN03171 169 GCFAGAAALRLAKDLAENNRGARVLVVAAEITLLLFNGPDEGCFQTLLNQGLFGDGAAAVIVGADADAA--ERPLFEIVS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 248 AAQTILPDSDGAIDGHLREVGLTFHL-LKDVPGLISKNIEKSLDEAFKPL----GISDWNSIFWIAHPGGPAILDQVEIK 322
Cdd:PLN03171 247 AAQAIIPESDDAINMHFTEGGLDGNIgTRQVPGLIGDNIERCLLDAFAPLlggdGGAEWNDLFWAVHPGSSAILDQVDAA 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 99923763 323 LGLKEEKMRATRHVMREYGNMSSACVLFILDEMRKKSAKdgVATTGEGLEWGVLFGFGPGLTVETV 388
Cdd:PLN03171 327 LGLEPEKLAASRRVLSDYGNMFGATVIFALDELRRQMEE--AAAAGAWPELGVMMAFGPGLTVDAM 390
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
21-388 |
5.56e-171 |
|
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: 481.34 E-value: 5.56e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 21 PAGILAIGTANPANYVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHVT--EEFLKENPNMcaymAPSLDA 98
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPEM----SPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 99 RQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRL 178
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 179 AKDLAENNRGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFSDGAAALIVGSDPDTSVGEKPIFEMVSAAQTILPDSDG 258
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRRERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 259 AIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFKPL--GISDWNSIFWIAHPGGPAILDQVEIKLGLKEEKMRATRHV 336
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 99923763 337 MREYGNMSSACVLFILDEMRKKSAKdgvattgEGLEWGVLFGFGPGLTVETV 388
Cdd:cd00831 315 LRRYGNMSSSSVLYVLAYMEAKGRV-------KRGDRGLLIAFGPGFTCESA 359
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
9-233 |
2.11e-147 |
|
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: 416.56 E-value: 2.11e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 9 LDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNM 88
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 89 CAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQG 168
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 99923763 169 CFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDP 233
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
20-386 |
2.56e-124 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 364.02 E-value: 2.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 20 GPAGILAIGTANPANYVIQAEYPDYYFRITNSEHmTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNMCAYMAPSLDAR 99
Cdd:PLN03169 20 GKATILALGKAFPSQLVPQEYLVDGYFRDTKCDD-PALKEKLERLCKTTTVKTRYVVMSKEILDKYPELATEGTPTIKQR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 100 QDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLA 179
Cdd:PLN03169 99 LDIANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEARLPGGDLYLAKQLGLSPDVQRVMLYFLGCSGGVAGLRVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 180 KDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPdTSVGEKPIFEMVSAAQTILPDSDGA 259
Cdd:PLN03169 179 KDIAENNPGSRVLLTTSETTILGFRPPSPDRPYDLVGAALFGDGAAAVIIGADP-IPVSESPFFELHTAIQQFLPGTEKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 260 IDGHLREVGLTFHLLKDVPGLISKNIE----KSLDEAfkPLGISDWNSIFWIAHPGGPAILDQVEIKLGLKEEKMRATRH 335
Cdd:PLN03169 258 IDGRLTEEGINFKLGRELPQKIEDNIEgfckKLMKKA--GLVEKDYNDLFWAVHPGGPAILNRLEKKLKLAPEKLECSRR 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 99923763 336 VMREYGNMSSACVLFILDEMRKKSAKDGvattGEGLEWGVLFGFGPGLTVE 386
Cdd:PLN03169 336 ALMDYGNVSSNTIVYVLEYMREELKKKG----EEDEEWGLILAFGPGITFE 382
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
24-388 |
3.78e-98 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 295.90 E-value: 3.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 24 ILAIGTANPANYVIQAEYPDYyFRITNSEHMTDLkEKFKRMCDKSTIRKRHMHVTEEFLKENPnmcaymapSLDARQDIV 103
Cdd:COG3424 4 ILSIATAVPPHRYTQEEIAEF-AAELFGLDERDR-RRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERNALY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 104 VVEVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLA 183
Cdd:COG3424 74 IEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 184 ENNRGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVGekpiFEMVSAAQTILPDSDGAIDGH 263
Cdd:COG3424 154 RADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPGPG----PRILAFRSYLIPDTEDVMGWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 264 LREVGLTFHLLKDVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKLGLKEEKMRATRHVMREYGNM 343
Cdd:COG3424 229 VGDTGFRMVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNM 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 99923763 344 SSACVLFILDE-MRKKSAKDGvattgeglEWGVLFGFGPGLTVETV 388
Cdd:COG3424 309 SSATVLFVLERlLEEGAPAPG--------ERGLAMAFGPGFTAELV 346
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
244-388 |
4.11e-89 |
|
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: 265.47 E-value: 4.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 244 EMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKL 323
Cdd:pfam02797 1 ELVSAAQTFLPNTDGVIDGHLTEEGLTFHLGRDVPQKIEENIEEFLKKAFEPLGISEWNSLFWIVHPGGPAILDRVETKL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 99923763 324 GLKEEKMRATRHVMREYGNMSSACVLFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETV 388
Cdd:pfam02797 81 GLEPEKLEASRRALMDYGNVSSATVLFILDEMRKKSLKKGLATTGEGLDWGVLLAFGPGLTFETV 145
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
107-388 |
8.25e-57 |
|
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: 186.50 E-value: 8.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 107 VPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLrPSVKRLMMYQqGCFAGGTVLRLAKDLAEN 185
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGeFSGAAGQLAYHLGI-SGGPAYSVNQ-ACATGLTALALAVQQVQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 186 NRGARVLVVCSEItavtfrgpsdthldslvgqALFSDGAAALIVGSDPDTSV-GEKPIFEMVSAAQTILPDSDgaidghl 264
Cdd:cd00327 85 GKADIVLAGGSEE-------------------FVFGDGAAAAVVESEEHALRrGAHPQAEIVSTAATFDGASM------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 265 revgltfhllkdVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKLGLKEEKMR--ATRHVMREYGN 342
Cdd:cd00327 139 ------------VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRspAVSATLIMTGH 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 99923763 343 MSSACVLFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETV 388
Cdd:cd00327 207 PLGAAGLAILDELLLMLEHEFIPPTPREPRTVLLLGFGLGGTNAAV 252
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
107-388 |
1.97e-55 |
|
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: 185.53 E-value: 1.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 107 VPKLGKEAAVKAIKEWG----QPKSKITHLVFCTTSGVD----------------------MPGADYQLTKLLGLrpSVK 160
Cdd:cd00825 11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgadamravgpyvvtkamFPGASGQIATPLGI--HGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 161 RLMMYQqGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDT------------HLDSLVGQALFSDGAAALI 228
Cdd:cd00825 89 AYDVSA-ACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAmgalstpekasrTFDAAADGFVFGDGAGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 229 VGSDPDTSV-GEKPIFEMVSAAQTIlpdsDGAIDGHLREVGltfhllkdvpglisKNIEKSLDEAFKPLGISDWNSIFWI 307
Cdd:cd00825 168 VEELEHALArGAHIYAEIVGTAATI----DGAGMGAFAPSA--------------EGLARAAKEALAVAGLTVWDIDYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 308 AHPGGPAILDQVEIKLGLKE--EKMRATRHVMREYGNMSSACVLFILDEMRKKSAKDGVA------------------TT 367
Cdd:cd00825 230 AHGTGTPIGDVKELKLLRSEfgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPpsihieeldeaglnivteTT 309
|
330 340
....*....|....*....|.
gi 99923763 368 GEGLEWGVLFGFGPGLTVETV 388
Cdd:cd00825 310 PRELRTALLNGFGLGGTNATL 330
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
21-386 |
9.16e-37 |
|
"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: 136.02 E-value: 9.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 21 PAGILAIGTANPANYVIQAEYPDYYFRITNsehmtdlkeKFKRMcdkstIRKRHMhvteEFLKENpnmcaymapsldarq 100
Cdd:cd00827 1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPG---------KYTTG-----IGQRHM----AGDDED--------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 101 divvveVPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLRPSvkRLMMYQQGCFAGGTVLRLA 179
Cdd:cd00827 48 ------VPTMAVEAARRALERAGIDPDDIGLLIVATESPIDkGKSAATYLAELLGLTNA--EAFDLKQACYGGTAALQLA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 180 KDLAENNRGARVLVVCSEItavtFRGPSDTHLDslvGQALFSDGAAALIVGSDPDtsvgeKPIFEMVSAAQTILPDSD-- 257
Cdd:cd00827 120 ANLVESGPWRYALVVASDI----ASYLLDEGSA---LEPTLGDGAAAMLVSRNPG-----ILAAGIVSTHSTSDPGYDfs 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 258 --GAIDGHLREVGLTFHLL--------KDVPGLISKNIEKSLDEAFKPLGISDWNSIFWIAHPGGPAILDQVEIKLGLKE 327
Cdd:cd00827 188 pyPVMDGGYPKPCKLAYAIrltaepagRAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLGGPP 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 328 EKMRATRH-VMREYGNMSSACVLFILDEMRKKsakdGVATTGEGLewgVLFGFGPGLTVE 386
Cdd:cd00827 268 EKASQTRWiLLRRVGNMYAASILLGLASLLES----GKLKAGDRV---LLFSYGSGFTAE 320
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
100-234 |
5.27e-15 |
|
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: 75.60 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 100 QDIVVvevpkLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDM--PGADYqLTKLLGLRPSVkRLMMYQQGCFAGGTVLR 177
Cdd:COG3425 49 EDAVT-----MAANAARRALDRAGIDPSDIGAVYVGTESGPDAskPIATY-VHGALGLPPNC-RAFELKFACYAGTAALQ 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 99923763 178 LAKDLAENNRGARVLVVCSEItavtfrgpSDTHLDSlVGQALFSDGAAALIVGSDPD 234
Cdd:COG3425 122 AALGWVASGPNKKALVIASDI--------ARYGPGS-AGEYTQGAGAVAMLVGADPR 169
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
110-384 |
5.05e-13 |
|
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: 69.11 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 110 LGKEAAVKAIKEWGQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLrpsvKRLMMY--QQGC--FAGGtvLRLAKDLAE 184
Cdd:cd00830 53 LAVEAAKKALEDAGIDADDIDLIIVATSTPDYlFPATACLVQARLGA----KNAAAFdiNAACsgFLYG--LSTAAGLIR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 185 NNRGARVLVVCSEITA--VTFRGPSdTHLdslvgqaLFSDGAAALIVGSDPDT---------SVGEKPIFEMVSAAQTIL 253
Cdd:cd00830 127 SGGAKNVLVVGAETLSriLDWTDRS-TAV-------LFGDGAGAVVLEATEEDpgildsvlgSDGSGADLLTIPAGGSRS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 254 PDSDGAIDGHL-----REVgltfhlLKDVPGLISKNIEKSLDEA-FKPLGIsDWnsiFWIaHPGGPAILDQVEIKLGLKE 327
Cdd:cd00830 199 PFEDAEGGDPYlvmdgREV------FKFAVRLMPESIEEALEKAgLTPDDI-DW---FVP-HQANLRIIEAVAKRLGLPE 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 99923763 328 EKMRatrHVMREYGNMSSACVLFILDEM-RKKSAKDGvattgeglEWGVLFGFGPGLT 384
Cdd:cd00830 268 EKVV---VNLDRYGNTSAASIPLALDEAiEEGKLKKG--------DLVLLLGFGAGLT 314
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
21-374 |
3.47e-11 |
|
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: 63.59 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 21 PAGILAIGTANPANyviqaeypdyyfRITNSE--HMTDL-KEKFKRmcdKSTIRKRHMHVTEEflkenpnMCAYMApsld 97
Cdd:COG0332 2 NVRILGTGSYLPER------------VVTNDDleKRLDTsDEWIEE---RTGIRERRIAAPDE-------TTSDLA---- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 98 arqdivvvevpklgKEAAVKAIKEWGQPKSKITHLVFCTTSGvDM--PGADYQLTKLLGLRpsvkrlmmyqqGCFA---- 171
Cdd:COG0332 56 --------------VEAARKALEAAGIDPEDIDLIIVATVTP-DYlfPSTACLVQHKLGAK-----------NAAAfdin 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 172 ---GGTV--LRLAKDLAENNRGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFSDGAAALIVGSDPDT---------S 236
Cdd:COG0332 110 aacSGFVyaLSVAAALIRSGQAKNVLVVGAETlSRIVDWTDRSTCV-------LFGDGAGAVVLEASEEGpgilgsvlgS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 237 VGEKPIFEMVSAAQTILPDSDGAI-DGHLREVGltfhllKDVPGLISKNIEKSLDEAFKPLGISdWNSIFWIA-HPGGPA 314
Cdd:COG0332 183 DGSGADLLVVPAGGSRNPPSPVDEgDHYLRMDG------REVFKFAVRNLPEVIREALEKAGLT-LDDIDWFIpHQANLR 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 99923763 315 ILDQVEIKLGLKEEKMRATrhvMREYGNMSSACVLFILDEM-RKKSAKDG----VATTGEGLEWG 374
Cdd:COG0332 256 IIEAVAKRLGLPEEKVVVN---IDRYGNTSAASIPLALDEAlREGRIKPGdlvlLAGFGAGLTWG 317
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
219-384 |
1.46e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 52.56 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 219 LFSDGAAALIVGSDPDT---------SVGEKPIFEMVSAAQTILPDSDGAIDGHLREVGLTfhLLKDVPGLISKNIEKSL 289
Cdd:PRK12879 158 LFGDGAGAVVLEATENEpgfidyvlgTDGDGGDILYRTGLGTTMDRDALSGDGYIVQNGRE--VFKWAVRTMPKGARQVL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 290 DEAfkplGIS----DWnsifWIAHPGGPAILDQVEIKLGLKEEKmraTRHVMREYGNMSSACVLFILDEMRkksaKDGVA 365
Cdd:PRK12879 236 EKA----GLTkddiDW----VIPHQANLRIIESLCEKLGIPMEK---TLVSVEYYGNTSAATIPLALDLAL----EQGKI 300
|
170
....*....|....*....
gi 99923763 366 TTGEGLewgVLFGFGPGLT 384
Cdd:PRK12879 301 KPGDTL---LLYGFGAGLT 316
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
110-348 |
2.60e-07 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 51.76 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 110 LGKEAAVKAIKEWGQPKSKITHLV-FCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRG 188
Cdd:PRK07204 55 MGAEAAKKAVEDAKLTLDDIDCIIcASGTIQQAIPCTASLIQEQLGLQHSGIPCFDINSTCLSFITALDTISYAIECGRY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 189 ARVLVVCSEITAVtfrGPSDTHLDSLVgqaLFSDGAAALIVGSDPDTS---------VGEKPIFEMVSAAQTILPDSDGA 259
Cdd:PRK07204 135 KRVLIISSEISSV---GLNWGQNESCI---LFGDGAAAVVITKGDHSSrilashmetYSSGAHLSEIRGGGTMIHPREYS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 260 IDghlREVGLTFHLL-KDVPGLISKNIEKSLDEAFKPLGISdWNSIFW-IAHPGGPAILDQVEIKLGLKEEKMRAtrhVM 337
Cdd:PRK07204 209 EE---RKEDFLFDMNgRAIFKLSSKYLMKFIDKLLMDAGYT-LADIDLiVPHQASGPAMRLIRKKLGVDEERFVT---IF 281
|
250
....*....|.
gi 99923763 338 REYGNMSSACV 348
Cdd:PRK07204 282 EDHGNMIAASI 292
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
155-380 |
8.10e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 50.73 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 155 LRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLdsLVGQALFSDGAAALIVGSDPD 234
Cdd:PLN02854 236 LRTDIKSYNLGGMGCSAGLISIDLANDLLKANPNSYAVVVSTENITLNWYFGNDRSM--LLCNCIFRMGGAAVLLSNKAR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 235 TSVGEKpiFEMVSAAQTilpdSDGAIDGHLR------------EVGLTFHLLKDVPGLISKNI----------------- 285
Cdd:PLN02854 314 DRKRSK--YQLVHTVRT----HKGADDKNYNcvyqreddkgtiGVSLARELMAVAGDALKTNIttlgplvlplseqfmff 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 286 -----EKSLDEAFKPLgISDWNSIF--WIAHPGGPAILDQVEIKLGLKEEKMRATRHVMREYGNMSSACVLFildEMRKK 358
Cdd:PLN02854 388 vtlvrRKLLKAKVKPY-IPDFKLAFehFCIHAGGRAVLDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWY---ELAYT 463
|
250 260
....*....|....*....|..
gi 99923763 359 SAKdGVATTGEGLeWGVLFGFG 380
Cdd:PLN02854 464 EAK-GRVSAGDRV-WQIAFGSG 483
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
300-384 |
1.30e-06 |
|
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: 45.95 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 300 DWnsiFWIaHPGGPAILDQVEIKLGLKEEKMRATrhvMREYGNMSSACVLFILDEM-RKKSAKDGvattgeglEWGVLFG 378
Cdd:pfam08541 12 DW---FVP-HQANLRIIDAVAKRLGLPPEKVVVN---LDEYGNTSAASIPLALDEAvEEGKLKPG--------DLVLLVG 76
|
....*.
gi 99923763 379 FGPGLT 384
Cdd:pfam08541 77 FGAGLT 82
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
219-384 |
7.00e-05 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 44.29 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 219 LFSDGAAALIVGSDPDT--------SVGEKPIFEMVSAAQTILPDSDGAI--DGhlREVgltFhllKDVPGLISKNIEKS 288
Cdd:PRK09352 157 LFGDGAGAVVLGASEEPgilsthlgSDGSYGDLLYLPGGGSRGPASPGYLrmEG--REV---F---KFAVRELAKVAREA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 289 LDEAfkplGIS----DWnsifWIAHPGGPAILDQVEIKLGLKEEKMRATrhvMREYGNMSSACVLFILDEMrkksAKDGV 364
Cdd:PRK09352 229 LEAA----GLTpediDW----LVPHQANLRIIDATAKKLGLPMEKVVVT---VDKYGNTSAASIPLALDEA----VRDGR 293
|
170 180
....*....|....*....|
gi 99923763 365 ATTGEGLewgVLFGFGPGLT 384
Cdd:PRK09352 294 IKRGDLV---LLEGFGGGLT 310
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
155-358 |
7.61e-05 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 44.68 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 155 LRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSE-ITAVTFRGpSDTHLdsLVGQALFSDGAAALIVGSDP 233
Cdd:PLN00415 182 LKTDVKTYNLSGMGCSAGAISVDLATNLLKANPNTYAVIVSTEnMTLSMYRG-NDRSM--LVPNCLFRVGGAAVMLSNRS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 234 DTSVGEKpiFEMVSAAQTilpdSDGAIDGHLRevglTFHLLKDVPGLISKNIEK--------SLDEAFKPLG-------- 297
Cdd:PLN00415 259 QDRVRSK--YELTHIVRT----HKGSSDKHYT----CAEQKEDSKGIVGVALSKeltvvagdTLKTNLTALGplvlplse 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 298 ---------------------ISDWNSIF--WIAHPGGPAILDQVEIKLGLKEEKMRATRHVMREYGNMSSACVLFILDE 354
Cdd:PLN00415 329 klrfilflvksklfrlkvspyVPDFKLCFkhFCIHAGGRALLDAVEKGLGLSEFDLEPSRMTLHRFGNTSSSSLWYELAY 408
|
....
gi 99923763 355 MRKK 358
Cdd:PLN00415 409 VEAK 412
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
166-238 |
2.67e-04 |
|
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: 39.42 E-value: 2.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 99923763 166 QQGCfAGGTV-LRLAKDLAENNRGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFSDGAAALIVGSDPDTSVG 238
Cdd:pfam08545 4 NAAC-SGFVYaLSTAAALIRSGRAKNVLVIGAETlSKILDWTDRSTAV-------LFGDGAGAVVLEATDEPGAR 70
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
219-374 |
3.01e-04 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 42.42 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 219 LFSDGAAALIVGS--DPDTSV----------GEKPIFEMVSAAQTILPDSDGAIDGHLREVGLTFHLL----KDVPGLIS 282
Cdd:PLN02326 200 LFGDGAGAVVLQAcdDDEDGLlgfdmhsdgnGHKHLHATFKGEDDDSSGGNTNGVGDFPPKKASYSCIqmngKEVFKFAV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 283 KNIEKSLDEAFKPLGISDwNSIFW-IAHPGGPAILDQVEIKLGLKEEKMRATrhvMREYGNMSSACVLFILDE-MR--KK 358
Cdd:PLN02326 280 RCVPQVIESALQKAGLTA-ESIDWlLLHQANQRIIDAVAQRLGIPPEKVISN---LANYGNTSAASIPLALDEaVRsgKV 355
|
170
....*....|....*...
gi 99923763 359 SAKDGVATT--GEGLEWG 374
Cdd:PLN02326 356 KKGDVIATAgfGAGLTWG 373
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
154-246 |
3.17e-04 |
|
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: 42.23 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 154 GLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSE-ITAVTFRGpSDTHLdsLVGQALFSDGAAALIVGSD 232
Cdd:pfam08392 130 KLRSDIKSYNLSGMGCSAGLISIDLAKNLLQVHPNTYALVVSTEnITPNWYFG-NDRSM--LLPNCLFRMGGAAVLLSNR 206
|
90
....*....|....
gi 99923763 233 PDTSVGEKpiFEMV 246
Cdd:pfam08392 207 PADRRRAK--YELV 218
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
168-380 |
1.92e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 40.34 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 168 GCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLdsLVGQALFSDGAAALIVG---SD--------PDTS 236
Cdd:PLN02192 237 GCSAGLISIDLAKHLLQVHPNSYALVISMENITLNWYFGNDRSM--LVSNCLFRMGGAAILLSnkrSDrrrskyqlVHTV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 237 VGEKPIFEMVSAAQTILPDSDGAIDghlreVGLTFHLLKDVPGLISKNI----------------------EKSLDEAFK 294
Cdd:PLN02192 315 RTHKGADDKCFACVTQEEDSAGKIG-----VSLSKDLMAVAGDALKTNIttlgplvlpmseqllffatlvgKKLFKMKLK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99923763 295 PLgISDWNSIF--WIAHPGGPAILDQVEIKLGLKEEKMRATRHVMREYGNMSSACVLFildEMRKKSAKdGVATTGEGLe 372
Cdd:PLN02192 390 PY-IPDFKLAFehFCIHAGGRAVLDELEKNLQLSDWHMEPSRMTLYRFGNTSSSSLWY---ELAYSEAK-GRIKKGDRT- 463
|
....*...
gi 99923763 373 WGVLFGFG 380
Cdd:PLN02192 464 WQIAFGSG 471
|
|
| |
