|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
1-516 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 1061.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 1 MDGAGESRlggdgggdgsvgvqIRQTRMLPDFLQSVNLKYVKLGYHYLISNLLTLCLFPLAVVISVEASQMNPDDLKQLW 80
Cdd:PLN02377 1 MDSGGEIR--------------IHQTRMLPDFLQSVNLKYVKLGYHYLISNLLTLCFIPLIIIISIEASQMNPDDLRQLW 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 81 IHLQYNLVSIIICSAILVFGLTVYVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFDDSALEFQRKILERSGL 160
Cdd:PLN02377 67 IHLQYNLVSIIICSAFLVFGLTVYIMTRPRPVYLVDYSCYRAPDHLKAPFARFMEHSRLTGDFDDSSLEFQRKILERSGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 161 GEDTYVPEAMHYVPPRISMAAAREEAEQVMFGALDNLFANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRS 240
Cdd:PLN02377 147 GEDTYVPEAMHYIPPRPSMAAAREEAEQVMFGALDNLFANTNVNPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 241 YNLGGMGCSAGVIAVDLAKDMLLVHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRL 320
Cdd:PLN02377 227 FNLGGMGCSAGVIAVDLAKDMLQVHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYKL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 321 VHVVRTHRGADDKAFRCVYQEQDDTGRTGVSLSKDLMAIAGETLKTNITTLGPLVLPISEQILFFMTLVVKKLFNGKVKP 400
Cdd:PLN02377 307 VHVVRTHRGADDKAFRCVYQEQDDAGKTGVSLSKDLMAIAGEALKTNITTLGPLVLPISEQLLFFATLVVKKLFNKKMKP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 401 YIPDFKLAFEHFCIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGS 480
Cdd:PLN02377 387 YIPDFKLAFDHFCIHAGGRAVIDELEKNLQLLPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRKGNRVWQIAFGS 466
|
490 500 510
....*....|....*....|....*....|....*.
gi 15223556 481 GFKCNSAIWEALRHVKPSNNSPWEDCIDKYPVTLSY 516
Cdd:PLN02377 467 GFKCNSAVWEALRHVKPSNNSPWEDCIDKYPVKLVY 502
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
104-393 |
0e+00 |
|
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: 573.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 104 YVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFDDSALEFQRKILERSGLGEDTYVPEAMHYVPPRISMAAAR 183
Cdd:pfam08392 1 YLARRPRPVYLVDYSCYKPPDDRKVSTETFMEHIQRNGHLDLESLDFQRKILERSGLGEETYLPRAVLEGPPDPTLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 184 EEAEQVMFGALDNLFANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDLAKDMLL 263
Cdd:pfam08392 81 EEAEEVIFGAVDDLFAKTGVSPRDIDILVVNCSLFNPTPSLSAMIVNRYKLRSDIKSYNLSGMGCSAGLISIDLAKNLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 264 VHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRLVHVVRTHRGADDKAFRCVYQEQD 343
Cdd:pfam08392 161 VHPNTYALVVSTENITPNWYFGNDRSMLLPNCLFRMGGAAVLLSNRPADRRRAKYELVHTVRTHKGADDRAYNCVYQEED 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15223556 344 DTGRTGVSLSKDLMAIAGETLKTNITTLGPLVLPISEQILFFMTLVVKKL 393
Cdd:pfam08392 241 EDGKVGVSLSKDLMKVAGRALKTNITTLGPLVLPLSEQLRFAATLLARKL 290
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
94-489 |
9.36e-149 |
|
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: 430.11 E-value: 9.36e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 94 SAILVFGlTVYVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFddsalefQRKILERSGlGEDTYVP----EA 169
Cdd:cd00831 2 ATILAIG-TAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGI-------ETRYLVLPG-GEETYAPrpemSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 170 MHYVPPRISMAAAREEAEQVMFGALDNLFantnVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCS 249
Cdd:cd00831 73 SLDERNDIALEEARELAEEAARGALDEAG----LRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 250 AGVIAVDLAKDMLLVHRNTYAVVVSTENITQnWYFGN-KKSMLIPNCLFRVGGSAVLLSNKSRDKRRskyrlvhvvRTHR 328
Cdd:cd00831 149 AGAIALDLAKDLLEANPGARVLVVSTELCSL-WYRGPdHRSMLVGNALFGDGAAAVLLSNDPRDRRR---------ERPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 329 GADDKAFRCVYQeqDDTGRTGVSLSKDLMAIagetlktnitTLGPLVLPISEQilfFMTLVVKKLFngkVKPYIPDFKLA 408
Cdd:cd00831 219 FELVRAASTLLP--DSEDAMGWHLGEEGLTF----------VLSRDVPRLVEK---NLERVLRKLL---ARLGIGLFKLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 409 FEHFCIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAI 488
Cdd:cd00831 281 FDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFTCESAV 360
|
.
gi 15223556 489 W 489
Cdd:cd00831 361 W 361
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
179-482 |
3.49e-34 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 131.80 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 179 MAAAREEAEQVMFGALDNLFANTNVKPKDIG-ILVVNCSLFNpTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDL 257
Cdd:COG3424 70 NALYIEEALELAEEAARRALDKAGLDPEDIDhLVTVSCTGFA-APGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 258 AKDMLLVHRNTYAVVVSTENITQNWYFGN-KKSMLIPNCLFRVGGSAVLLSnkSRDKRRSKYRLVHvVRTHR---GADDK 333
Cdd:COG3424 149 AADFLRADPDAVVLVVCVELCSLTFQRDDdSKDNLVANALFGDGAAAVVVS--GDPRPGPGPRILA-FRSYLipdTEDVM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 334 AFRCVyqeqdDTGrTGVSLSKDLMAIAGETLKTNITT-LGPLVLPISEqilffmtlvvkklfngkvkpyipdfklaFEHF 412
Cdd:COG3424 226 GWDVG-----DTG-FRMVLSPEVPDLIAEHLAPAVEPlLARHGLTIED----------------------------IDHW 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 413 CIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGF 482
Cdd:COG3424 272 AVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGF 341
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
180-488 |
3.05e-13 |
|
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: 70.49 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 180 AAAREEAEQVMFGALDNLFANTNVKPKDI-GILVVNCSLFNPTPSLSAMIVNKYKLRgNIRSYNLGGmGCSAGVIAVDLA 258
Cdd:TIGR00747 45 AADDETSSTMGFEAAKRAIENAGISKDDIdLIIVATTTPDHAFPSAACMVQAYLGIK-GIPAFDLSA-ACAGFIYALSVA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 259 KDMLLVHRNTYAVVVSTENITQ--NWYFGNkksmlipNC-LFRVGGSAVLLSNKSRDKRrskyrlvhVVRTHRGADDKAF 335
Cdd:TIGR00747 123 KQYIESGKYKTVLVVGAEKLSStlDWTDRG-------TCvLFGDGAGAVVLGESEDPGG--------IISTHLGADGTQG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 336 RCVYQEQDDTGRTGvslSKDLMAIAG-ETLKTNITTLGplvlpiseqilffmTLVVKKLFNGKVKPYIPDFklafehFCI 414
Cdd:TIGR00747 188 EALYLPAGGRPTSG---PSPFITMEGnEVFKHAVRKMG--------------DVVEETLEANGLDPEDIDW------FVP 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15223556 415 HAGGRAVIDELEKNLQLSPVHVEAsrmTLHRFGNTSSSSIwyELAYIEAK--GRMRRGNRVWQIAFGSGFKCNSAI 488
Cdd:TIGR00747 245 HQANLRIIEALAKRLELDMSQVVK---TVHKYGNTSAASI--PLALDELLrtGRIKPGDLLLLVAFGGGLTWGAAL 315
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
1-516 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 1061.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 1 MDGAGESRlggdgggdgsvgvqIRQTRMLPDFLQSVNLKYVKLGYHYLISNLLTLCLFPLAVVISVEASQMNPDDLKQLW 80
Cdd:PLN02377 1 MDSGGEIR--------------IHQTRMLPDFLQSVNLKYVKLGYHYLISNLLTLCFIPLIIIISIEASQMNPDDLRQLW 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 81 IHLQYNLVSIIICSAILVFGLTVYVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFDDSALEFQRKILERSGL 160
Cdd:PLN02377 67 IHLQYNLVSIIICSAFLVFGLTVYIMTRPRPVYLVDYSCYRAPDHLKAPFARFMEHSRLTGDFDDSSLEFQRKILERSGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 161 GEDTYVPEAMHYVPPRISMAAAREEAEQVMFGALDNLFANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRS 240
Cdd:PLN02377 147 GEDTYVPEAMHYIPPRPSMAAAREEAEQVMFGALDNLFANTNVNPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 241 YNLGGMGCSAGVIAVDLAKDMLLVHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRL 320
Cdd:PLN02377 227 FNLGGMGCSAGVIAVDLAKDMLQVHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYKL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 321 VHVVRTHRGADDKAFRCVYQEQDDTGRTGVSLSKDLMAIAGETLKTNITTLGPLVLPISEQILFFMTLVVKKLFNGKVKP 400
Cdd:PLN02377 307 VHVVRTHRGADDKAFRCVYQEQDDAGKTGVSLSKDLMAIAGEALKTNITTLGPLVLPISEQLLFFATLVVKKLFNKKMKP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 401 YIPDFKLAFEHFCIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGS 480
Cdd:PLN02377 387 YIPDFKLAFDHFCIHAGGRAVIDELEKNLQLLPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRKGNRVWQIAFGS 466
|
490 500 510
....*....|....*....|....*....|....*.
gi 15223556 481 GFKCNSAIWEALRHVKPSNNSPWEDCIDKYPVTLSY 516
Cdd:PLN02377 467 GFKCNSAVWEALRHVKPSNNSPWEDCIDKYPVKLVY 502
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
22-512 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 811.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 22 QIRQTRMLPDFLQSVNLKYVKLGYHYLISNLLTLCLFPLAVVISVEASQMNPDDLKQLWIHLQYNLVSIIICSAILVFGL 101
Cdd:PLN02192 12 EPSSSRKLPDFKKSVKLKYVKLGYHYLITHGMYLFLSPLVVVIAAQLSTFSIQDLHDLWEHLKFNLISVILCSTLLVFLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 102 TVYVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFDDSALEFQRKILERSGLGEDTYVPEAMHYVPPRISMAA 181
Cdd:PLN02192 92 TLYFLTRPRPVYLVDFSCYKPDDSRKCTRKIFMDRSKLTGSFTEENLEFQRKILERSGLGESTYLPEAVLNVPPNPCMAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 182 AREEAEQVMFGALDNLFANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDLAKDM 261
Cdd:PLN02192 172 ARKEAETVMFGAIDQLLAKTSVKPKDIGILIVNCSLFNPTPSLSAMVINHYKLRGNILSYNLGGMGCSAGLISIDLAKHL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 262 LLVHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRLVHVVRTHRGADDKAFRCVYQE 341
Cdd:PLN02192 252 LQVHPNSYALVISMENITLNWYFGNDRSMLVSNCLFRMGGAAILLSNKRSDRRRSKYQLVHTVRTHKGADDKCFACVTQE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 342 QDDTGRTGVSLSKDLMAIAGETLKTNITTLGPLVLPISEQILFFMTLVVKKLFNGKVKPYIPDFKLAFEHFCIHAGGRAV 421
Cdd:PLN02192 332 EDSAGKIGVSLSKDLMAVAGDALKTNITTLGPLVLPMSEQLLFFATLVGKKLFKMKLKPYIPDFKLAFEHFCIHAGGRAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 422 IDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAIWEALRHVKPSN-N 500
Cdd:PLN02192 412 LDELEKNLQLSDWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWKALRTVNPAKeK 491
|
490
....*....|..
gi 15223556 501 SPWEDCIDKYPV 512
Cdd:PLN02192 492 NPWMDEIHEFPV 503
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
23-512 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 746.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 23 IRQTRMLPDFLQSVNLKYVKLGYHY---LISNLLTLCLFPLAVVISVEASQMNPDDLKQLWIH--LQYNLVSIIICSAIL 97
Cdd:PLN02854 20 IKIRQRLPDFLQSVKLKYVKLGYGYscnPATILFFLIILPLTIATLVQITGLEFDTVSELWSNqaLHLDTATRLTGSAFL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 98 VFGLTVYVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFDDSALEFQRKILERSGLGEDTYVPEAMHYVPPRI 177
Cdd:PLN02854 100 LFLLGLYWAKRSKPVYLVDFACYKPEDERKISVDSFLTMTEENGSFEDETVQFQRRISTRSGLGDETYLPRGITSRPPNL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 178 SMAAAREEAEQVMFGALDNLFANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDL 257
Cdd:PLN02854 180 CMEEARAEAEAVMFGALDSLFSKTGVKPRDIGILIVNCSLFNPTPSLSAMIVNHYKLRTDIKSYNLGGMGCSAGLISIDL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 258 AKDMLLVHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRLVHVVRTHRGADDKAFRC 337
Cdd:PLN02854 260 ANDLLKANPNSYAVVVSTENITLNWYFGNDRSMLLCNCIFRMGGAAVLLSNKARDRKRSKYQLVHTVRTHKGADDKNYNC 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 338 VYQEQDDTGRTGVSLSKDLMAIAGETLKTNITTLGPLVLPISEQILFFMTLVVKKLFNGKVKPYIPDFKLAFEHFCIHAG 417
Cdd:PLN02854 340 VYQREDDKGTIGVSLARELMAVAGDALKTNITTLGPLVLPLSEQFMFFVTLVRRKLLKAKVKPYIPDFKLAFEHFCIHAG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 418 GRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAIWEALRHV-- 495
Cdd:PLN02854 420 GRAVLDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWYELAYTEAKGRVSAGDRVWQIAFGSGFKCNSAVWKALREIpt 499
|
490
....*....|....*..
gi 15223556 496 KPSNNSPWEDCIDKYPV 512
Cdd:PLN02854 500 GESTGNPWADSIDRYPV 516
|
|
| PLN02932 |
PLN02932 |
3-ketoacyl-CoA synthase |
45-514 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 178520 Cd Length: 478 Bit Score: 722.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 45 YHYLISNLLTLCLFPLAVVISVEASQMNPDDLKQLWIHLQYNLVSIIICSAILVFGLTVYVMTRPRPVYLVDFSCYLPPD 124
Cdd:PLN02932 1 FNYLMAHRFKLCFLPLMVGIAMEASRLSTQDLQNFYLYLQNNLTSLTMFFLYLALGSTLYLMTRPKPVYLVDFSCYLPPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 125 HLKAPYARFMEHSRLTGDF------DDSALEFQRKILERSGLGEDTYVPEAMHYVPPRISMAAAREEAEQVMFGALDNLF 198
Cdd:PLN02932 81 HLKASIQTIMGHVRRVREAgawkqeSDYLMDFCEKILERSGLGQETYIPEGLQCLPLQQNLAVSRKETEEVIIGAVDNLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 199 ANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDLAKDMLLVHRNTYAVVVSTENI 278
Cdd:PLN02932 161 RNTGISPSDIGILVVNSSTFNPTPSLSSILVNKFKLRDNIKSLNLGGMGCSAGVIAIDAAKSLLQVHRNTYALVVSTENI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 279 TQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRLVHVVRTHRGADDKAFRCVYQEQDDTGRTGVSLSKDLMA 358
Cdd:PLN02932 241 TQNLYLGNNKSMLVTNCLFRIGGAAILLSNRSRDRKRAKYELVHTVRVHTGADDRSYECATQEEDEDGIVGVSLSKNLPM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 359 IAGETLKTNITTLGPLVLPISEQILFFMTLVVKKLFNGKVKPYIPDFKLAFEHFCIHAGGRAVIDELEKNLQLSPVHVEA 438
Cdd:PLN02932 321 VAARTLKINIATLGPLVLPLSEKFHFFVRFVKKKFFNPKLKHYIPDFKLAFEHFCIHAGGRALIDEMEKNLHLTPLDVEA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15223556 439 SRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAIWEALRHVKPSNNSPWEDCIDKYPVTL 514
Cdd:PLN02932 401 SRMTLHRFGNTSSSSIWYELAYTEAKGRMKKGDRIWQIALGSGFKCNSSVWVALRNVKPSANNPWEDCLHKYPVEI 476
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
104-393 |
0e+00 |
|
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: 573.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 104 YVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFDDSALEFQRKILERSGLGEDTYVPEAMHYVPPRISMAAAR 183
Cdd:pfam08392 1 YLARRPRPVYLVDYSCYKPPDDRKVSTETFMEHIQRNGHLDLESLDFQRKILERSGLGEETYLPRAVLEGPPDPTLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 184 EEAEQVMFGALDNLFANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDLAKDMLL 263
Cdd:pfam08392 81 EEAEEVIFGAVDDLFAKTGVSPRDIDILVVNCSLFNPTPSLSAMIVNRYKLRSDIKSYNLSGMGCSAGLISIDLAKNLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 264 VHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRLVHVVRTHRGADDKAFRCVYQEQD 343
Cdd:pfam08392 161 VHPNTYALVVSTENITPNWYFGNDRSMLLPNCLFRMGGAAVLLSNRPADRRRAKYELVHTVRTHKGADDRAYNCVYQEED 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15223556 344 DTGRTGVSLSKDLMAIAGETLKTNITTLGPLVLPISEQILFFMTLVVKKL 393
Cdd:pfam08392 241 EDGKVGVSLSKDLMKVAGRALKTNITTLGPLVLPLSEQLRFAATLLARKL 290
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
104-515 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 528.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 104 YVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFDDSALEFQRKILERSGLGEDTYVPEAMHYVPPRISMAAAR 183
Cdd:PLN00415 52 YSTTRSKPVYLVDFSCHQPTDSCKISSETFFNMAKGAQLYTEETIQFMTRILNRSGLGDDTYSPRCMLTSPPTPSMYEAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 184 EEAEQVMFGALDNLFANTNVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDLAKDMLL 263
Cdd:PLN00415 132 HESELVIFGALNSLFKKTGIEPREVGIFIVNCSLFNPNPSLSSMIVNRYKLKTDVKTYNLSGMGCSAGAISVDLATNLLK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 264 VHRNTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYRLVHVVRTHRGADDKAFRCVYQEQD 343
Cdd:PLN00415 212 ANPNTYAVIVSTENMTLSMYRGNDRSMLVPNCLFRVGGAAVMLSNRSQDRVRSKYELTHIVRTHKGSSDKHYTCAEQKED 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 344 DTGRTGVSLSKDLMAIAGETLKTNITTLGPLVLPISEQILFFMTLVVKKLFNGKVKPYIPDFKLAFEHFCIHAGGRAVID 423
Cdd:PLN00415 292 SKGIVGVALSKELTVVAGDTLKTNLTALGPLVLPLSEKLRFILFLVKSKLFRLKVSPYVPDFKLCFKHFCIHAGGRALLD 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 424 ELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAIWEALRHVkPSNNS-- 501
Cdd:PLN00415 372 AVEKGLGLSEFDLEPSRMTLHRFGNTSSSSLWYELAYVEAKCRVKRGDRVWQLAFGSGFKCNSIVWRALRTI-PANESlv 450
|
410
....*....|....*.
gi 15223556 502 --PWEDCIDKYPVTLS 515
Cdd:PLN00415 451 gnPWGDSVHKYPVHVT 466
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
94-489 |
9.36e-149 |
|
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: 430.11 E-value: 9.36e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 94 SAILVFGlTVYVMTRPRPVYLVDFSCYLPPDHLKAPYARFMEHSRLTGDFddsalefQRKILERSGlGEDTYVP----EA 169
Cdd:cd00831 2 ATILAIG-TAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGI-------ETRYLVLPG-GEETYAPrpemSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 170 MHYVPPRISMAAAREEAEQVMFGALDNLFantnVKPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCS 249
Cdd:cd00831 73 SLDERNDIALEEARELAEEAARGALDEAG----LRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 250 AGVIAVDLAKDMLLVHRNTYAVVVSTENITQnWYFGN-KKSMLIPNCLFRVGGSAVLLSNKSRDKRRskyrlvhvvRTHR 328
Cdd:cd00831 149 AGAIALDLAKDLLEANPGARVLVVSTELCSL-WYRGPdHRSMLVGNALFGDGAAAVLLSNDPRDRRR---------ERPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 329 GADDKAFRCVYQeqDDTGRTGVSLSKDLMAIagetlktnitTLGPLVLPISEQilfFMTLVVKKLFngkVKPYIPDFKLA 408
Cdd:cd00831 219 FELVRAASTLLP--DSEDAMGWHLGEEGLTF----------VLSRDVPRLVEK---NLERVLRKLL---ARLGIGLFKLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 409 FEHFCIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAI 488
Cdd:cd00831 281 FDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFTCESAV 360
|
.
gi 15223556 489 W 489
Cdd:cd00831 361 W 361
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
179-482 |
3.49e-34 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 131.80 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 179 MAAAREEAEQVMFGALDNLFANTNVKPKDIG-ILVVNCSLFNpTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDL 257
Cdd:COG3424 70 NALYIEEALELAEEAARRALDKAGLDPEDIDhLVTVSCTGFA-APGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 258 AKDMLLVHRNTYAVVVSTENITQNWYFGN-KKSMLIPNCLFRVGGSAVLLSnkSRDKRRSKYRLVHvVRTHR---GADDK 333
Cdd:COG3424 149 AADFLRADPDAVVLVVCVELCSLTFQRDDdSKDNLVANALFGDGAAAVVVS--GDPRPGPGPRILA-FRSYLipdTEDVM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 334 AFRCVyqeqdDTGrTGVSLSKDLMAIAGETLKTNITT-LGPLVLPISEqilffmtlvvkklfngkvkpyipdfklaFEHF 412
Cdd:COG3424 226 GWDVG-----DTG-FRMVLSPEVPDLIAEHLAPAVEPlLARHGLTIED----------------------------IDHW 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 413 CIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGF 482
Cdd:COG3424 272 AVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGF 341
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
111-482 |
6.41e-16 |
|
"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: 78.63 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 111 PVYLVDFSCYLPPDHLKApyaRFMEHsrltGDFDDSALeFQRKILERSGLGEDTYVPEamhyvpprISMAAAReeaeqvm 190
Cdd:cd00827 1 DVGIEAIGAYLPRYRVDN---EELAE----GLGVDPGK-YTTGIGQRHMAGDDEDVPT--------MAVEAAR------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 191 fgaldNLFANTNVKPKDIG-ILVVNCSLFNPTPSlSAMIVNKYKLRGNIRSYNLGGmGCSAGVIAVDLAKDMLLVHRNTY 269
Cdd:cd00827 58 -----RALERAGIDPDDIGlLIVATESPIDKGKS-AATYLAELLGLTNAEAFDLKQ-ACYGGTAALQLAANLVESGPWRY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 270 AVVVSTENITQNWYFGNKksmliPNCLFRVGGSAVLLSNKSRDKRRskyrlvHVVRTHRGADDKAFRCVYQEQDDTGRTG 349
Cdd:cd00827 131 ALVVASDIASYLLDEGSA-----LEPTLGDGAAAMLVSRNPGILAA------GIVSTHSTSDPGYDFSPYPVMDGGYPKP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 350 VSLSKDlmaiagetlktnittlGPLVLPISEQILF--FMTLVVKKLFNGKVKPYIPDfklAFEHFCIH-AGGRAVIDELE 426
Cdd:cd00827 200 CKLAYA----------------IRLTAEPAGRAVFeaAHKLIAKVVRKALDRAGLSE---DIDYFVPHqPNGKKILEAVA 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15223556 427 KNLQLSPVHVEASRMT-LHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGF 482
Cdd:cd00827 261 KKLGGPPEKASQTRWIlLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGF 317
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
180-488 |
3.05e-13 |
|
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: 70.49 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 180 AAAREEAEQVMFGALDNLFANTNVKPKDI-GILVVNCSLFNPTPSLSAMIVNKYKLRgNIRSYNLGGmGCSAGVIAVDLA 258
Cdd:TIGR00747 45 AADDETSSTMGFEAAKRAIENAGISKDDIdLIIVATTTPDHAFPSAACMVQAYLGIK-GIPAFDLSA-ACAGFIYALSVA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 259 KDMLLVHRNTYAVVVSTENITQ--NWYFGNkksmlipNC-LFRVGGSAVLLSNKSRDKRrskyrlvhVVRTHRGADDKAF 335
Cdd:TIGR00747 123 KQYIESGKYKTVLVVGAEKLSStlDWTDRG-------TCvLFGDGAGAVVLGESEDPGG--------IISTHLGADGTQG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 336 RCVYQEQDDTGRTGvslSKDLMAIAG-ETLKTNITTLGplvlpiseqilffmTLVVKKLFNGKVKPYIPDFklafehFCI 414
Cdd:TIGR00747 188 EALYLPAGGRPTSG---PSPFITMEGnEVFKHAVRKMG--------------DVVEETLEANGLDPEDIDW------FVP 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15223556 415 HAGGRAVIDELEKNLQLSPVHVEAsrmTLHRFGNTSSSSIwyELAYIEAK--GRMRRGNRVWQIAFGSGFKCNSAI 488
Cdd:TIGR00747 245 HQANLRIIEALAKRLELDMSQVVK---TVHKYGNTSAASI--PLALDELLrtGRIKPGDLLLLVAFGGGLTWGAAL 315
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
193-490 |
2.78e-12 |
|
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: 67.83 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 193 ALDNLFANTNVKPKDIG-ILVVNCSLFNPTPSLSAMIVNKYKLRgNIRSYNLGGmGCSAGVIAVDLAKDMLLVHRNTYAV 271
Cdd:COG0332 58 AARKALEAAGIDPEDIDlIIVATVTPDYLFPSTACLVQHKLGAK-NAAAFDINA-ACSGFVYALSVAAALIRSGQAKNVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 272 VVSTENITQ--NW-------YFGNkksmlipnclfrvGGSAVLLSnKSRDKRRskyrlvhVVRTHRGADDKAFRCVYQEQ 342
Cdd:COG0332 136 VVGAETLSRivDWtdrstcvLFGD-------------GAGAVVLE-ASEEGPG-------ILGSVLGSDGSGADLLVVPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 343 DDTGR--TGVSLSKDLMAIAGETL-KTNITTLGPLVlpisEQILffmtlvvKKlfNGkvkpyipdfkLAFE---HFCIHA 416
Cdd:COG0332 195 GGSRNppSPVDEGDHYLRMDGREVfKFAVRNLPEVI----REAL-------EK--AG----------LTLDdidWFIPHQ 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15223556 417 GGRAVIDELEKNLQLSPvhvEASRMTLHRFGNTSSSSIwyELAYIEA--KGRMRRGNRVWQIAFGSGFKCNSAIWE 490
Cdd:COG0332 252 ANLRIIEAVAKRLGLPE---EKVVVNIDRYGNTSAASI--PLALDEAlrEGRIKPGDLVLLAGFGAGLTWGAAVLR 322
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
154-489 |
2.04e-11 |
|
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: 65.25 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 154 ILERSGLGEdtyvpeamhyvpPRIsmAAAREEAEQVMFGALDNLFANTNVKPKDIG-ILVVNCSLFNPTPSLSAMIVNKY 232
Cdd:cd00830 32 IRTRTGIRE------------RRI--ADPGETTSDLAVEAAKKALEDAGIDADDIDlIIVATSTPDYLFPATACLVQARL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 233 KLrGNIRSYNLGGmGCSAGVIAVDLAKDMLLVHRNTYAVVVSTENITQNWYFGNKKSmlipnC-LFRVGGSAVLLSnKSR 311
Cdd:cd00830 98 GA-KNAAAFDINA-ACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRST-----AvLFGDGAGAVVLE-ATE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 312 DKRrskyrlvHVVRTHRGADDKAFRCVYqeqddTGRTGVSLSKDLMAIAGETLKTNittlGPLVLpisEQILFFMTLVVK 391
Cdd:cd00830 170 EDP-------GILDSVLGSDGSGADLLT-----IPAGGSRSPFEDAEGGDPYLVMD----GREVF---KFAVRLMPESIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 392 KLF--NGkvkpYIPDfklAFEHFCIHAGGRAVIDELEKNLQLSPVHVEasrMTLHRFGNTSSSSIWYELAYIEAKGRMRR 469
Cdd:cd00830 231 EALekAG----LTPD---DIDWFVPHQANLRIIEAVAKRLGLPEEKVV---VNLDRYGNTSAASIPLALDEAIEEGKLKK 300
|
330 340
....*....|....*....|
gi 15223556 470 GNRVWQIAFGSGFKCNSAIW 489
Cdd:cd00830 301 GDLVLLLGFGAGLTWGAALL 320
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
411-490 |
8.23e-11 |
|
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: 58.28 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 411 HFCIHAGGRAVIDELEKNLQLSPvhvEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAIWE 490
Cdd:pfam08541 13 WFVPHQANLRIIDAVAKRLGLPP---EKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAGLTWGAALLR 89
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
414-481 |
2.51e-09 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 59.33 E-value: 2.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15223556 414 IHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAY-IEAKGRMRRGNRVWQI--AFGSG 481
Cdd:PLN03169 308 VHPGGPAILNRLEKKLKLAPEKLECSRRALMDYGNVSSNTIVYVLEYmREELKKKGEEDEEWGLilAFGPG 378
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
207-495 |
6.84e-09 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 57.71 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 207 DIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSYNLGGMGCSAGVIAVDLAKDMLLVHRNTYAVVVSTEnITQNWYFGN 286
Cdd:PLN03171 129 DITHLVVTTNSGAHIPGVDFRLVPLLGLRPSVRRTMLHLNGCFAGAAALRLAKDLAENNRGARVLVVAAE-ITLLLFNGP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 287 KKS---MLIPNCLFRVGGSAVLLSNKSRDKRRSKYRLVHVVRTHRGADDKAFRCVYQEQddtGRTGVSLSKDLMAIAGET 363
Cdd:PLN03171 208 DEGcfqTLLNQGLFGDGAAAVIVGADADAAERPLFEIVSAAQAIIPESDDAINMHFTEG---GLDGNIGTRQVPGLIGDN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 364 LKTNIT-TLGPLVlpiseqilffmtlvvkklfNGKVKPYIPDFklafeHFCIHAGGRAVIDELEKNLQLSPVHVEASRMT 442
Cdd:PLN03171 285 IERCLLdAFAPLL-------------------GGDGGAEWNDL-----FWAVHPGSSAILDQVDAALGLEPEKLAASRRV 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 443 LHRFGNTSSSSIWYELAyiEAKGRMRRGNR--VW-----QIAFGSGFKCNSAIWEALRHV 495
Cdd:PLN03171 341 LSDYGNMFGATVIFALD--ELRRQMEEAAAagAWpelgvMMAFGPGLTVDAMLLHASGHP 398
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
358-481 |
2.03e-08 |
|
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: 53.22 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 358 AIAGETLKTNIT-TLGPLVLP-ISEQILFFMTLVVKKLfngkvkpYIPDFKLAFehFCIHAGGRAVIDELEKNLQLSPVH 435
Cdd:pfam02797 16 VIDGHLTEEGLTfHLGRDVPQkIEENIEEFLKKAFEPL-------GISEWNSLF--WIVHPGGPAILDRVETKLGLEPEK 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15223556 436 VEASRMTLHRFGNTSSSSIWYELAYI---EAKGRMRRGNRV--WQI--AFGSG 481
Cdd:pfam02797 87 LEASRRALMDYGNVSSATVLFILDEMrkkSLKKGLATTGEGldWGVllAFGPG 139
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
234-481 |
9.01e-06 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 48.15 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 234 LRGNIRSYNLGGMGCSAGVIAVDLAKDMLLVHRNTYAVVVSTEnITQNWYFGNKKS---MLIPNCLFRVGGSAVLL-SNK 309
Cdd:PLN03173 150 LRSSVKRFMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-ITAVTFRGPSDThldSLVGQALFGDGAAAIIIgSDP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 310 SRDKRRSKYRLVHVVRTHRGADDKAFRCVYQEqddtgrtgVSLSKDLMAIAGETLKTNIttlgplvlpiseqilffmtlv 389
Cdd:PLN03173 229 VLGVEKPLFELVSAAQTILPDSDGAIDGHLRE--------VGLTFHLLKDVPGLISKNV--------------------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 390 vKKLFNGKVKPY-IPDFKLAFehFCIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAK---- 464
Cdd:PLN03173 280 -EKSLTEAFKPLgISDWNSLF--WIAHPGGPAILDQVEAKLALKPEKLRATRHVLSEYGNMSSACVLFILDEMRKKsaed 356
|
250
....*....|....*...
gi 15223556 465 GRMRRGNRV-WQIAFGSG 481
Cdd:PLN03173 357 GLKSTGEGLeWGVLFGFG 374
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
390-464 |
2.35e-05 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 46.57 E-value: 2.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15223556 390 VKKLFNGKVKPY-IPDFKLAFehFCIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAK 464
Cdd:PLN03168 278 IEKFLNEARKCVgSPDWNEMF--WAVHPGGPAILDQVEAKLKLTKDKMQGSRDILSEFGNMSSASVLFVLDQIRQR 351
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
422-482 |
2.45e-04 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 43.14 E-value: 2.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15223556 422 IDELEKNLQLSPvhvEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGF 482
Cdd:PRK09352 252 IDATAKKLGLPM---EKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGL 309
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
234-481 |
5.72e-04 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 42.35 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 234 LRGNIRSYNLGGMGCSAGVIAVDLAKDMLLVHRNTYAVVVSTEnITQNWYFGNKKSML---IPNCLFRVGGSAVLLSNKS 310
Cdd:PLN03172 150 LKPSVKRFMMYQQGCFAGGTVLRLAKDLAENNAGSRVLVVCSE-ITAVTFRGPSDTHLdslVGQALFGDGAAAVIIGADP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 311 RDK-RRSKYRLVHVVRT----HRGADDKAFRcvyqeqdDTGRTgVSLSKDLMAIAGETLKTNITTLgplVLPISeqilff 385
Cdd:PLN03172 229 DTKiERPLFEIVSAAQTilpdSDGAIDGHLR-------EVGLT-FHLLKDVPGLISKNIEKSLVEA---FAPIG------ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223556 386 mtlvvkklfngkvkpyIPDFKLAFehFCIHAGGRAVIDELEKNLQLSPVHVEASRMTLHRFGNTSSSSIWYELAYIEAK- 464
Cdd:PLN03172 292 ----------------INDWNSIF--WIAHPGGPAILDQVEIKLDLKEEKLRATRHVLSDYGNMSSACVLFILDEMRKKs 353
|
250 260
....*....|....*....|.
gi 15223556 465 ---GRMRRGNRV-WQIAFGSG 481
Cdd:PLN03172 354 ieeGKGSTGEGLeWGVLFGFG 374
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
411-489 |
5.83e-03 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 38.93 E-value: 5.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15223556 411 HFCIHAGGRAVIDELEKNLQLSPvhvEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRRGNRVWQIAFGSGFKCNSAIW 489
Cdd:PRK05963 249 RFFPHQANARIVDKVCETIGIPR---AKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAVVM 324
|
|
| |
