|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
7-394 |
0e+00 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 715.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 7 PSLEEIRKAQRADGPAGILGIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKENP 86
Cdd:PLN03172 2 PSIAEIRKAQRAEGPATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKENP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 87 DMCAYMAPSLDVRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQ 166
Cdd:PLN03172 82 NMCAYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMYQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 167 QGCYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGADPDASVgEKPIFEMV 246
Cdd:PLN03172 162 QGCFAGGTVLRLAKDLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKI-ERPLFEIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 247 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKLGLK 326
Cdd:PLN03172 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12002443 327 EEKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKEDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 394
Cdd:PLN03172 321 EEKLRATRHVLSDYGNMSSACVLFILDEMRKKSIEEGKGSTGEGLEWGVLFGFGPGLTVETVVLHSVP 388
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
2-394 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 704.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 2 VMGTQPSLEEIRKAQRADGPAGILGIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEF 81
Cdd:PLN03170 1 MAGATVTVEEVRKAQRATGPATVLAIGTATPANCVHQADYPDYYFRITKSEHMTELKEKFKRMCDKSQIRKRYMHLTEEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 82 LKENPDMCAYMAPSLDVRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKR 161
Cdd:PLN03170 81 LAENPNMCAYMAPSLDARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 162 LMMYQQGCYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGADPDASVgEKP 241
Cdd:PLN03170 161 LMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSESHLDSMVGQALFGDGAAAVIVGADPDERV-ERP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 242 IFEMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVEL 321
Cdd:PLN03170 240 LFQLVSASQTILPDSEGAIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12002443 322 KLGLKEEKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKEDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 394
Cdd:PLN03170 320 KVGLEKERMRATRHVLSEYGNMSSACVLFILDEMRKRSAEDGQATTGEGFDWGVLFGFGPGLTVETVVLHSVP 392
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
8-393 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 700.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 8 SLEEIRKAQRADGPAGILGIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKENPD 87
Cdd:PLN03173 3 TVDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKENPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 88 MCAYMAPSLDVRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQ 167
Cdd:PLN03173 83 VCEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMYQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 168 GCYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGADPDASVgEKPIFEMVS 247
Cdd:PLN03173 163 GCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGV-EKPLFELVS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 248 AAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKLGLKE 327
Cdd:PLN03173 242 AAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALKP 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12002443 328 EKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKEDGVATTGEGLEWGVLFGFGPGLTVETVVLHSV 393
Cdd:PLN03173 322 EKLRATRHVLSEYGNMSSACVLFILDEMRKKSAEDGLKSTGEGLEWGVLFGFGPGLTVETVVLHSV 387
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
13-394 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 563.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 13 RKAQRADGPAGILGIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKENPDMCAYM 92
Cdd:PLN03168 7 RGQPRAEGPACVLGIGTAVPPAEFLQSEYPDFFFNITNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVLKANPGICTYM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 93 APSLDVRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCYAG 172
Cdd:PLN03168 87 EPSLNVRHDIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGADHALAKLLGLKPTVKRVMMYQTGCFGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 173 GTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGADPDASVgEKPIFEMVSAAQTI 252
Cdd:PLN03168 167 ASVLRVAKDLAENNKGARVLAVASEVTAVTYRAPSENHLDGLVGSALFGDGAGVYVVGSDPKPEV-EKALFEVHWAGETI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 253 LPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKLGLKEEKMRA 332
Cdd:PLN03168 246 LPESDGAIDGHLTEAGLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQG 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12002443 333 TRHVLSEYGNMSSACVLFIMDEMRRKSKEDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 394
Cdd:PLN03168 326 SRDILSEFGNMSSASVLFVLDQIRQRSVKMGASTLGEGSEFGFFIGFGPGLTLEVLVLRAAA 387
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
3-392 |
6.15e-175 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 493.37 E-value: 6.15e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 3 MGTQ---PSLEEIRKAQRADGPAGILGIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTE 79
Cdd:PLN03171 1 MGSAaapANLGEICRAQRADGLAAVLAIGTANPANCVPQDEFPDFYFRATKSDHLTALKDKFKRICQELGVQKRYLHHTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 80 EFLKENPDMCAYMAPSLDVRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSV 159
Cdd:PLN03171 81 ELLSAHPEFLDHDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAHIPGVDFRLVPLLGLRPSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 160 KRLMMYQQGCYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGADPDASvgE 239
Cdd:PLN03171 161 RRTMLHLNGCFAGAAALRLAKDLAENNRGARVLVVAAEITLLLFNGPDEGCFQTLLNQGLFGDGAAAVIVGADADAA--E 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 240 KPIFEMVSAAQTILPDSDGAIDGHLREVGLTFHL-LKDVPGLISKNIEKSLEEAFKPL----GISDWNSLFWIAHPGGPA 314
Cdd:PLN03171 239 RPLFEIVSAAQAIIPESDDAINMHFTEGGLDGNIgTRQVPGLIGDNIERCLLDAFAPLlggdGGAEWNDLFWAVHPGSSA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12002443 315 ILDQVELKLGLKEEKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKEdgVATTGEGLEWGVLFGFGPGLTVETVVLHS 392
Cdd:PLN03171 319 ILDQVDAALGLEPEKLAASRRVLSDYGNMFGATVIFALDELRRQMEE--AAAAGAWPELGVMMAFGPGLTVDAMLLHA 394
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
21-390 |
1.57e-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: 488.27 E-value: 1.57e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 21 PAGILGIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLT--EEFLKENPDMcaymAPSLDV 98
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPEM----SPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 99 RQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCYAGGTVLRL 178
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 179 AKDLAENNRGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFSDGAAALIVGADPDASVGEKPIFEMVSAAQTILPDSDG 258
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRRERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 259 AIDGHLREVGLTFHLLKDVPGLISKNIEKSLEEAFKPL--GISDWNSLFWIAHPGGPAILDQVELKLGLKEEKMRATRHV 336
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 12002443 337 LSEYGNMSSACVLFIMDEMRRKSKEdgvattgEGLEWGVLFGFGPGLTVETVVL 390
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 ... |
9-233 |
2.93e-146 |
|
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: 413.86 E-value: 2.93e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 9 LEEIRKAQRADGPAGILGIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKENPDM 88
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 89 CAYMAPSLDVRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQG 168
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12002443 169 CYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGADP 233
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
1-393 |
2.90e-123 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 361.71 E-value: 2.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 1 MVMGTQPSLEEIRKAQRADGPAGILGIGTANPANHVIQAEYPDYYFRITNSEHmTDLKEKFKRMCDKSMIRKRHMHLTEE 80
Cdd:PLN03169 1 MSNGSSSASKAGSRRAANPGKATILALGKAFPSQLVPQEYLVDGYFRDTKCDD-PALKEKLERLCKTTTVKTRYVVMSKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 81 FLKENPDMCAYMAPSLDVRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVK 160
Cdd:PLN03169 80 ILDKYPELATEGTPTIKQRLDIANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEARLPGGDLYLAKQLGLSPDVQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 161 RLMMYQQGCYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGADPDAsVGEK 240
Cdd:PLN03169 160 RVMLYFLGCSGGVAGLRVAKDIAENNPGSRVLLTTSETTILGFRPPSPDRPYDLVGAALFGDGAAAVIIGADPIP-VSES 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 241 PIFEMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIE----KSLEEAfkPLGISDWNSLFWIAHPGGPAIL 316
Cdd:PLN03169 239 PFFELHTAIQQFLPGTEKTIDGRLTEEGINFKLGRELPQKIEDNIEgfckKLMKKA--GLVEKDYNDLFWAVHPGGPAIL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12002443 317 DQVELKLGLKEEKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKEDGvattGEGLEWGVLFGFGPGLTVETVVLHSV 393
Cdd:PLN03169 317 NRLEKKLKLAPEKLECSRRALMDYGNVSSNTIVYVLEYMREELKKKG----EEDEEWGLILAFGPGITFEGILARNL 389
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
24-391 |
1.08e-97 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 295.13 E-value: 1.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 24 ILGIGTANPANHVIQAEYPDYyFRITNSEHMTDLkEKFKRMCDKSMIRKRHMHLTEEFLKENPdmcaymapSLDVRQDIV 103
Cdd:COG3424 4 ILSIATAVPPHRYTQEEIAEF-AAELFGLDERDR-RRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERNALY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 104 VVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCYAGGTVLRLAKDLA 183
Cdd:COG3424 74 IEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 184 ENNRGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFSDGAAALIVGADPDASVGekpiFEMVSAAQTILPDSDGAIDGH 263
Cdd:COG3424 154 RADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPGPG----PRILAFRSYLIPDTEDVMGWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 264 LREVGLTFHLLKDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKLGLKEEKMRATRHVLSEYGNM 343
Cdd:COG3424 229 VGDTGFRMVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNM 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 12002443 344 SSACVLFIMDEMRrkskEDGVATTGeglEWGVLFGFGPGLTVETVVLH 391
Cdd:COG3424 309 SSATVLFVLERLL----EEGAPAPG---ERGLAMAFGPGFTAELVLLR 349
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
244-394 |
2.22e-92 |
|
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: 273.94 E-value: 2.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 244 EMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKL 323
Cdd:pfam02797 1 ELVSAAQTFLPNTDGVIDGHLTEEGLTFHLGRDVPQKIEENIEEFLKKAFEPLGISEWNSLFWIVHPGGPAILDRVETKL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12002443 324 GLKEEKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKEDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 394
Cdd:pfam02797 81 GLEPEKLEASRRALMDYGNVSSATVLFILDEMRKKSLKKGLATTGEGLDWGVLLAFGPGLTFETVVLRSVP 151
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
107-390 |
1.15e-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: 196.51 E-value: 1.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 107 VPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVD-MPGADYQLTKLLGLrPSVKRLMMYQqGCYAGGTVLRLAKDLAEN 185
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGeFSGAAGQLAYHLGI-SGGPAYSVNQ-ACATGLTALALAVQQVQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 186 NRGARVLVVCSEItavtfrgpsdthldslvgqALFSDGAAALIVGADPDASV-GEKPIFEMVSAAQTILPDSDgaidghl 264
Cdd:cd00327 85 GKADIVLAGGSEE-------------------FVFGDGAAAAVVESEEHALRrGAHPQAEIVSTAATFDGASM------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 265 revgltfhllkdVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKLGLKEEKMR--ATRHVLSEYGN 342
Cdd:cd00327 139 ------------VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRspAVSATLIMTGH 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 12002443 343 MSSACVLFIMDEMRRKSKEDGVATTGEGLEWGVLFGFGPGLTVETVVL 390
Cdd:cd00327 207 PLGAAGLAILDELLLMLEHEFIPPTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
107-390 |
5.01e-59 |
|
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: 194.78 E-value: 5.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 107 VPKLGKEAAVKAIKEWG----QPKSKITHVVFCTTSGVD----------------------MPGADYQLTKLLGLrpSVK 160
Cdd:cd00825 11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgadamravgpyvvtkamFPGASGQIATPLGI--HGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 161 RLMMYQqGCYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDT------------HLDSLVGQALFSDGAAALI 228
Cdd:cd00825 89 AYDVSA-ACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAmgalstpekasrTFDAAADGFVFGDGAGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 229 VGADPDASV-GEKPIFEMVSAAQTIlpdsDGAIDGHLREVGltfhllkdvpglisKNIEKSLEEAFKPLGISDWNSLFWI 307
Cdd:cd00825 168 VEELEHALArGAHIYAEIVGTAATI----DGAGMGAFAPSA--------------EGLARAAKEALAVAGLTVWDIDYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 308 AHPGGPAILDQVELKLGLKE--EKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKEDGVA------------------TT 367
Cdd:cd00825 230 AHGTGTPIGDVKELKLLRSEfgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPpsihieeldeaglnivteTT 309
|
330 340
....*....|....*....|...
gi 12002443 368 GEGLEWGVLFGFGPGLTVETVVL 390
Cdd:cd00825 310 PRELRTALLNGFGLGGTNATLVL 332
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
21-390 |
6.52e-39 |
|
"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: 141.80 E-value: 6.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 21 PAGILGIGTANPANHVIQAEYPDYYFRITNSEHMtdlkekfkrmcdksMIRKRHMHLTEEflkENPDMCAymapsldvrq 100
Cdd:cd00827 1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTT--------------GIGQRHMAGDDE---DVPTMAV---------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 101 divvvevpklgkEAAVKAIKEWGQPKSKITHVVFCTTSGVD-MPGADYQLTKLLGLRPSvkRLMMYQQGCYAGGTVLRLA 179
Cdd:cd00827 54 ------------EAARRALERAGIDPDDIGLLIVATESPIDkGKSAATYLAELLGLTNA--EAFDLKQACYGGTAALQLA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 180 KDLAENNRGARVLVVCSEItavtFRGPSDTHLDslvGQALFSDGAAALIVGADPDASvgekpIFEMVSAAQTILPDSD-- 257
Cdd:cd00827 120 ANLVESGPWRYALVVASDI----ASYLLDEGSA---LEPTLGDGAAAMLVSRNPGIL-----AAGIVSTHSTSDPGYDfs 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 258 --GAIDGHLREVGLTFHLL--------KDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKLGLKE 327
Cdd:cd00827 188 pyPVMDGGYPKPCKLAYAIrltaepagRAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLGGPP 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12002443 328 EKMRATRH-VLSEYGNMSSACVLFIMDEMRRKSKEDGvattGEGLewgVLFGFGPGLTVETVVL 390
Cdd:cd00827 268 EKASQTRWiLLRRVGNMYAASILLGLASLLESGKLKA----GDRV---LLFSYGSGFTAEAFVL 324
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
100-234 |
2.00e-16 |
|
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: 80.22 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 100 QDIVVvevpkLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDM--PGADYqLTKLLGLRPSVkRLMMYQQGCYAGGTVLR 177
Cdd:COG3425 49 EDAVT-----MAANAARRALDRAGIDPSDIGAVYVGTESGPDAskPIATY-VHGALGLPPNC-RAFELKFACYAGTAALQ 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 12002443 178 LAKDLAENNRGARVLVVCSEItavtfrgpSDTHLDSlVGQALFSDGAAALIVGADPD 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 ... |
22-390 |
5.53e-15 |
|
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: 75.27 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 22 AGILGIGTANPANhviqaeypdyyfRITNSE--HMTDLKEKFKRmcDKSMIRKRHMHLTEEFLkenPDMCAymapsldvr 99
Cdd:cd00830 2 ARILGIGSYLPER------------VVTNDEleKRLDTSDEWIR--TRTGIRERRIADPGETT---SDLAV--------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 100 qdivvvevpklgkEAAVKAIKEWGQPKSKITHVVFCTTSGVD-MPGADYQLTKLLGLrpsvKRLMMY--QQGC----YAg 172
Cdd:cd00830 56 -------------EAAKKALEDAGIDADDIDLIIVATSTPDYlFPATACLVQARLGA----KNAAAFdiNAACsgflYG- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 173 gtvLRLAKDLAENNRGARVLVVCSEITA--VTFRGPSdTHLdslvgqaLFSDGAAALIVGADPDA---------SVGEKP 241
Cdd:cd00830 118 ---LSTAAGLIRSGGAKNVLVVGAETLSriLDWTDRS-TAV-------LFGDGAGAVVLEATEEDpgildsvlgSDGSGA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 242 IFEMVSAAQTILPDSDGAIDGHL-----REVgltfhlLKDVPGLISKNIEKSLEEA-FKPLGIsDWnslFWIaHPGGPAI 315
Cdd:cd00830 187 DLLTIPAGGSRSPFEDAEGGDPYlvmdgREV------FKFAVRLMPESIEEALEKAgLTPDDI-DW---FVP-HQANLRI 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12002443 316 LDQVELKLGLKEEKMRatrHVLSEYGNMSSACVLFIMDEMRrkskEDGVATTGEGLewgVLFGFGPGLTVETVVL 390
Cdd:cd00830 256 IEAVAKRLGLPEEKVV---VNLDRYGNTSAASIPLALDEAI----EEGKLKKGDLV---LLLGFGAGLTWGAALL 320
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
21-374 |
1.05e-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: 65.13 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 21 PAGILGIGTANPANhviqaeypdyyfRITNSEhmtdlkekFKRMCDKSM--------IRKRHMHLTEEFLKenpDMCAym 92
Cdd:COG0332 2 NVRILGTGSYLPER------------VVTNDD--------LEKRLDTSDewieertgIRERRIAAPDETTS---DLAV-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 93 apsldvrqdivvvevpklgkEAAVKAIKEWGQPKSKITHVVFCTTSGvDM--PGADYQLTKLLGLrpsvKRLMMY--QQG 168
Cdd:COG0332 57 --------------------EAARKALEAAGIDPEDIDLIIVATVTP-DYlfPSTACLVQHKLGA----KNAAAFdiNAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 169 C----YAggtvLRLAKDLAENNRGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFSDGAAALIVGADPD--------- 234
Cdd:COG0332 112 CsgfvYA----LSVAAALIRSGQAKNVLVVGAETlSRIVDWTDRSTCV-------LFGDGAGAVVLEASEEgpgilgsvl 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 235 ASVGEKPIFEMVSAAQTILPDSDGAIDGHL-----REVgltfhlLKDVPGLISKNIEKSLEEAfkplGIS----DWnslf 305
Cdd:COG0332 181 GSDGSGADLLVVPAGGSRNPPSPVDEGDHYlrmdgREV------FKFAVRNLPEVIREALEKA----GLTlddiDW---- 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12002443 306 WIAHPGGPAILDQVELKLGLKEEKMRATrhvLSEYGNMSSACVLFIMDEMRRKSK-EDG----VATTGEGLEWG 374
Cdd:COG0332 247 FIPHQANLRIIEAVAKRLGLPEEKVVVN---IDRYGNTSAASIPLALDEALREGRiKPGdlvlLAGFGAGLTWG 317
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
219-384 |
1.30e-08 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 56.03 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 219 LFSDGAAALIVGADPDA---------SVGEKPIFEMVSAAQTILPDSDGAIDGHLREVGLTfhLLKDVPGLISKNIEKSL 289
Cdd:PRK12879 158 LFGDGAGAVVLEATENEpgfidyvlgTDGDGGDILYRTGLGTTMDRDALSGDGYIVQNGRE--VFKWAVRTMPKGARQVL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 290 EEAfkplGIS----DWnslfWIAHPGGPAILDQVELKLGLKEEKmraTRHVLSEYGNMSSACVLFIMDEMRrkskEDGVA 365
Cdd:PRK12879 236 EKA----GLTkddiDW----VIPHQANLRIIESLCEKLGIPMEK---TLVSVEYYGNTSAATIPLALDLAL----EQGKI 300
|
170
....*....|....*....
gi 12002443 366 TTGEGLewgVLFGFGPGLT 384
Cdd:PRK12879 301 KPGDTL---LLYGFGAGLT 316
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
24-348 |
3.61e-07 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 51.37 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 24 ILGIGTANPANHVIQAEYpdyyfritnsEHMTDLKEKFKRmcDKSMIRKRHMHLTEeflkenpdMCAYMapsldvrqdiv 103
Cdd:PRK07204 7 IKGIGTYLPKRKVDSLEL----------DKKLDLPEGWVL--KKSGVKTRHFVDGE--------TSSYM----------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 104 vvevpklGKEAAVKAIKEWGQPKSKITHVV-FCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCYAGGTVLRLAKDL 182
Cdd:PRK07204 56 -------GAEAAKKAVEDAKLTLDDIDCIIcASGTIQQAIPCTASLIQEQLGLQHSGIPCFDINSTCLSFITALDTISYA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 183 AENNRGARVLVVCSEITAVtfrGPSDTHLDSLVgqaLFSDGAAALIVGADPDAS---------VGEKPIFEMVSAAQTIL 253
Cdd:PRK07204 129 IECGRYKRVLIISSEISSV---GLNWGQNESCI---LFGDGAAAVVITKGDHSSrilashmetYSSGAHLSEIRGGGTMI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 254 PDSDGAIDghlREVGLTFHLL-KDVPGLISKNIEKSLEEAFKPLGISDWNSLFWIAHPGGPAILDQVELKLGLKEEKMRA 332
Cdd:PRK07204 203 HPREYSEE---RKEDFLFDMNgRAIFKLSSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVT 279
|
330
....*....|....*.
gi 12002443 333 trhVLSEYGNMSSACV 348
Cdd:PRK07204 280 ---IFEDHGNMIAASI 292
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
110-390 |
7.37e-07 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 50.46 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 110 LGKEAAVKAIKEWGQPKSKITHVVFCTTSGVD-MPGADYQLTKLLGLRPSVkrLMMYQQGC----YAggtvLRLAKDLAE 184
Cdd:PRK09352 55 LATEAAKKALEAAGIDPEDIDLIIVATTTPDYaFPSTACLVQARLGAKNAA--AFDLSAACsgfvYA----LSTADQFIR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 185 NNRGARVLVVCSEI-----------TAVtfrgpsdthldslvgqaLFSDGAAALIVGADPDA--------SVGEKPIFEM 245
Cdd:PRK09352 129 SGAYKNVLVIGAEKlsrivdwtdrsTCV-----------------LFGDGAGAVVLGASEEPgilsthlgSDGSYGDLLY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 246 VSAAQTILPDSDGAI--DGhlREVgltFhllKDVPGLISKNIEKSLEEAfkplGIS----DWnslfWIAHPGGPAILDQV 319
Cdd:PRK09352 192 LPGGGSRGPASPGYLrmEG--REV---F---KFAVRELAKVAREALEAA----GLTpediDW----LVPHQANLRIIDAT 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12002443 320 ELKLGLKEEKMRATrhvLSEYGNMSSACVLFIMDEMRRkskeDGVATTGEGLewgVLFGFGPGLTVETVVL 390
Cdd:PRK09352 256 AKKLGLPMEKVVVT---VDKYGNTSAASIPLALDEAVR----DGRIKRGDLV---LLEGFGGGLTWGAALV 316
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
110-374 |
1.53e-06 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 49.74 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 110 LGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKrlmmYQQGCYAGGTVLRL--AKDLAENNR 187
Cdd:PLN02326 99 LAVEAAKKALEMAGVDPEDVDLVLLCTSSPDDLFGSAPQVQAALGCTNALA----FDLTAACSGFVLGLvtAARFIRGGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 188 GARVLVV----CSEITAVTFRGPSdthldslvgqALFSDGAAALIVGA--DPDASV----------GEKPIFEMVSAAQT 251
Cdd:PLN02326 175 YKNVLVIgadaLSRYVDWTDRGTC----------ILFGDGAGAVVLQAcdDDEDGLlgfdmhsdgnGHKHLHATFKGEDD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 252 ILPDSDGAIDGHLREVGLTFHLL------------KDVPglisKNIEKSLEEAFKPLGISDWNSLfwiaHPGGPAILDQV 319
Cdd:PLN02326 245 DSSGGNTNGVGDFPPKKASYSCIqmngkevfkfavRCVP----QVIESALQKAGLTAESIDWLLL----HQANQRIIDAV 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 320 ELKLGLKEEKMRATrhvLSEYGNMSSACVLFIMDEMRRKSK---EDGVATT--GEGLEWG 374
Cdd:PLN02326 317 AQRLGIPPEKVISN---LANYGNTSAASIPLALDEAVRSGKvkkGDVIATAgfGAGLTWG 373
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
155-380 |
2.77e-06 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 49.18 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 155 LRPSVKRLMMYQQGCYAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLdsLVGQALFSDGAAALIVGADPD 234
Cdd:PLN02854 236 LRTDIKSYNLGGMGCSAGLISIDLANDLLKANPNSYAVVVSTENITLNWYFGNDRSM--LLCNCIFRMGGAAVLLSNKAR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 235 ASVGEKpiFEMVSAAQTilpdSDGAIDGHLR------------EVGLTFHLLKDVPGLISKNI----------------- 285
Cdd:PLN02854 314 DRKRSK--YQLVHTVRT----HKGADDKNYNcvyqreddkgtiGVSLARELMAVAGDALKTNIttlgplvlplseqfmff 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 286 -----EKSLEEAFKPLgISDWNSLF--WIAHPGGPAILDQVELKLGLKEEKMRATRHVLSEYGNMSSACVLFIMDEMRRK 358
Cdd:PLN02854 388 vtlvrRKLLKAKVKPY-IPDFKLAFehFCIHAGGRAVLDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWYELAYTEAK 466
|
250 260
....*....|....*....|..
gi 12002443 359 skedGVATTGEGLeWGVLFGFG 380
Cdd:PLN02854 467 ----GRVSAGDRV-WQIAFGSG 483
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
300-390 |
3.50e-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: 44.80 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 300 DWnslFWIaHPGGPAILDQVELKLGLKEEKMRATrhvLSEYGNMSSACVLFIMDEMRrkskEDGVATTGEGLewgVLFGF 379
Cdd:pfam08541 12 DW---FVP-HQANLRIIDAVAKRLGLPPEKVVVN---LDEYGNTSAASIPLALDEAV----EEGKLKPGDLV---LLVGF 77
|
90
....*....|.
gi 12002443 380 GPGLTVETVVL 390
Cdd:pfam08541 78 GAGLTWGAALL 88
|
|
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
155-380 |
7.14e-06 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 48.09 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 155 LRPSVKRLMMYQQGCYAGGTVLRLAKDLAENNRGARVLVVCSE-ITAVTFRGPSDThldSLVGQALFSDGAAALIV---- 229
Cdd:PLN02377 220 LRGNIRSFNLGGMGCSAGVIAVDLAKDMLQVHRNTYAVVVSTEnITQNWYFGNKKS---MLIPNCLFRVGGSAVLLsnks 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 230 ------------------GADPDASvgeKPIFEM--------VSAAQTILPDSDGAIDGHLREVG-LTFHLLKDVPGLIS 282
Cdd:PLN02377 297 rdkrrskyklvhvvrthrGADDKAF---RCVYQEqddagktgVSLSKDLMAIAGEALKTNITTLGpLVLPISEQLLFFAT 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 283 KNIEKSLEEAFKPLgISDWNSLF--WIAHPGGPAILDQVELKLGLKEEKMRATRHVLSEYGNMSSACV---LFIMDEMRR 357
Cdd:PLN02377 374 LVVKKLFNKKMKPY-IPDFKLAFdhFCIHAGGRAVIDELEKNLQLLPVHVEASRMTLHRFGNTSSSSIwyeLAYIEAKGR 452
|
250 260
....*....|....*....|...
gi 12002443 358 KSKEDGVattgegleWGVLFGFG 380
Cdd:PLN02377 453 MRKGNRV--------WQIAFGSG 467
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
124-380 |
5.33e-05 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 45.07 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 124 QPKSKITHVVFCTTSGVDmPGADYQLTKLLGLRPSVKRLMMYQQGCYAGGTVLRLAKDLAENNRGARVLVVCSE-ITAVT 202
Cdd:PLN00415 152 EPREVGIFIVNCSLFNPN-PSLSSMIVNRYKLKTDVKTYNLSGMGCSAGAISVDLATNLLKANPNTYAVIVSTEnMTLSM 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 203 FRGpSDTHLdsLVGQALFSDGAAALIVGADPDASVGEKpiFEMVSAAQTilpdSDGAIDGHLRevglTFHLLKDVPGLIS 282
Cdd:PLN00415 231 YRG-NDRSM--LVPNCLFRVGGAAVMLSNRSQDRVRSK--YELTHIVRT----HKGSSDKHYT----CAEQKEDSKGIVG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 283 KNIEK--------SLEEAFKPLG-----------------------------ISDWNSLF--WIAHPGGPAILDQVELKL 323
Cdd:PLN00415 298 VALSKeltvvagdTLKTNLTALGplvlplseklrfilflvksklfrlkvspyVPDFKLCFkhFCIHAGGRALLDAVEKGL 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 12002443 324 GLKEEKMRATRHVLSEYGNMSSACVLFIMDEMRRKSKedgvATTGEGLeWGVLFGFG 380
Cdd:PLN00415 378 GLSEFDLEPSRMTLHRFGNTSSSSLWYELAYVEAKCR----VKRGDRV-WQLAFGSG 429
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
166-238 |
7.54e-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: 40.96 E-value: 7.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12002443 166 QQGCyAGGTV-LRLAKDLAENNRGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFSDGAAALIVGADPDASVG 238
Cdd:pfam08545 4 NAAC-SGFVYaLSTAAALIRSGRAKNVLVIGAETlSKILDWTDRSTAV-------LFGDGAGAVVLEATDEPGAR 70
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
154-246 |
1.18e-03 |
|
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: 40.31 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12002443 154 GLRPSVKRLMMYQQGCYAGGTVLRLAKDLAENNRGARVLVVCSE-ITAVTFRGpSDTHLdsLVGQALFSDGAAALIVGAD 232
Cdd:pfam08392 130 KLRSDIKSYNLSGMGCSAGLISIDLAKNLLQVHPNTYALVVSTEnITPNWYFG-NDRSM--LLPNCLFRMGGAAVLLSNR 206
|
90
....*....|....
gi 12002443 233 PDASVGEKpiFEMV 246
Cdd:pfam08392 207 PADRRRAK--YELV 218
|
|
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