|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
1-509 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 1079.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 1 MDVEQKKPLIE-SSDRNLPDFKKSVKLKYVKLGYHYLITHGMYLFLSPLVLVIAAQISTFSVTDLRSLWEHLQYNLISVV 79
Cdd:PLN02192 2 SEVNQKTPLIEpSSSRKLPDFKKSVKLKYVKLGYHYLITHGMYLFLSPLVVVIAAQLSTFSIQDLHDLWEHLKFNLISVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 80 VCSMLLVFLMTIYFMTRPRPVYLVNFSCFKPDESRKCTKKIFMDRSKLTGSFTEENLEFQRKILQRSGLGESTYLPEAVL 159
Cdd:PLN02192 82 LCSTLLVFLSTLYFLTRPRPVYLVDFSCYKPDDSRKCTRKIFMDRSKLTGSFTEENLEFQRKILERSGLGESTYLPEAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 160 NVPPNPCMKEARKEAETVMFGAIDELLAKTNVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLGGMGCSAG 239
Cdd:PLN02192 162 NVPPNPCMAEARKEAETVMFGAIDQLLAKTSVKPKDIGILIVNCSLFNPTPSLSAMVINHYKLRGNILSYNLGGMGCSAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 240 LISIDLAKHLLHSIPNTYAMVISMENITLNWYFGNDRSKLVSNCLFRMGGAAILLSNKRWDRRRSKYELVDTVRTHKGAD 319
Cdd:PLN02192 242 LISIDLAKHLLQVHPNSYALVISMENITLNWYFGNDRSMLVSNCLFRMGGAAILLSNKRSDRRRSKYQLVHTVRTHKGAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 320 DKCFGCITQEEDSASKIGVTLSKELMAVAGDALKTNITTLGPLVLPTSEQLLFFATLVGRKLFKMKIKPYIPDFKLAFEH 399
Cdd:PLN02192 322 DKCFACVTQEEDSAGKIGVSLSKDLMAVAGDALKTNITTLGPLVLPMSEQLLFFATLVGKKLFKMKLKPYIPDFKLAFEH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 400 FCIHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGFKCNSSVWRA 479
Cdd:PLN02192 402 FCIHAGGRAVLDELEKNLQLSDWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWKA 481
|
490 500 510
....*....|....*....|....*....|
gi 15225767 480 VRSVNPKKEKNPWMDEIHEFPVEVPKVSTI 509
Cdd:PLN02192 482 LRTVNPAKEKNPWMDEIHEFPVDVPKVSTI 511
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
92-381 |
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: 564.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 92 YFMTRPRPVYLVNFSCFKPDESRKCTKKIFMDRSKLTGSFTEENLEFQRKILQRSGLGESTYLPEAVLNVPPNPCMKEAR 171
Cdd:pfam08392 1 YLARRPRPVYLVDYSCYKPPDDRKVSTETFMEHIQRNGHLDLESLDFQRKILERSGLGEETYLPRAVLEGPPDPTLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 172 KEAETVMFGAIDELLAKTNVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLH 251
Cdd:pfam08392 81 EEAEEVIFGAVDDLFAKTGVSPRDIDILVVNCSLFNPTPSLSAMIVNRYKLRSDIKSYNLSGMGCSAGLISIDLAKNLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 252 SIPNTYAMVISMENITLNWYFGNDRSKLVSNCLFRMGGAAILLSNKRWDRRRSKYELVDTVRTHKGADDKCFGCITQEED 331
Cdd:pfam08392 161 VHPNTYALVVSTENITPNWYFGNDRSMLLPNCLFRMGGAAVLLSNRPADRRRAKYELVHTVRTHKGADDRAYNCVYQEED 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15225767 332 SASKIGVTLSKELMAVAGDALKTNITTLGPLVLPTSEQLLFFATLVGRKL 381
Cdd:pfam08392 241 EDGKVGVSLSKDLMKVAGRALKTNITTLGPLVLPLSEQLRFAATLLARKL 290
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
77-477 |
1.28e-141 |
|
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: 411.62 E-value: 1.28e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 77 SVVVCSMLLVFLMTIYFMTRPRPVYLVNFSCFKPDESRKCTKKIFmdrskltgsfteENLEFQRKILQRSGlGESTYLP- 155
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLC------------AKTGIETRYLVLPG-GEETYAPr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 156 ---EAVLNVPPNPCMKEARKEAETVMFGAIDELLaktnVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLG 232
Cdd:cd00831 68 pemSPSLDERNDIALEEARELAEEAARGALDEAG----LRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 233 GMGCSAGLISIDLAKHLLHSIPNTYAMVISMENITLnWYFGND-RSKLVSNCLFRMGGAAILLSNKRWDRR--RSKYELV 309
Cdd:cd00831 144 GMGCSAGAIALDLAKDLLEANPGARVLVVSTELCSL-WYRGPDhRSMLVGNALFGDGAAAVLLSNDPRDRRreRPLFELV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 310 DTVRTHKgaddkcfgcitqeEDSASKIGVTLSKELMAVagdalktnitTLGPLVLPTSEQLLFFatlVGRKLFKmkiKPY 389
Cdd:cd00831 223 RAASTLL-------------PDSEDAMGWHLGEEGLTF----------VLSRDVPRLVEKNLER---VLRKLLA---RLG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 390 IPDFKLAFEHFCIHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSG 469
Cdd:cd00831 274 IGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPG 353
|
....*...
gi 15225767 470 FKCNSSVW 477
Cdd:cd00831 354 FTCESAVW 361
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
181-470 |
8.13e-35 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 133.73 E-value: 8.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 181 AIDELLAKTNVNPKDIGILI-VNCSLFNpTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLHSIPNTYAM 259
Cdd:COG3424 84 AARRALDKAGLDPEDIDHLVtVSCTGFA-APGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFLRADPDAVVL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 260 VISMENITLNWYFGND-RSKLVSNCLFRMGGAAILLSNKrwDRRRSKYELVDTvRTHkgaddkcfgCITQEED------S 332
Cdd:COG3424 163 VVCVELCSLTFQRDDDsKDNLVANALFGDGAAAVVVSGD--PRPGPGPRILAF-RSY---------LIPDTEDvmgwdvG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 333 ASKIGVTLSKELMAVAGDALKTNITTLgplvlptseqllffatLVGRKLFKMKIkpyipdfklafEHFCIHAGGRAVLDE 412
Cdd:COG3424 231 DTGFRMVLSPEVPDLIAEHLAPAVEPL----------------LARHGLTIEDI-----------DHWAVHPGGPKVLDA 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15225767 413 LEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGF 470
Cdd:COG3424 284 VEEALGLPPEALAHSREVLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGF 341
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
179-478 |
1.52e-11 |
|
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: 65.48 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 179 FGAIDELLAKTNVNPKDIGILIV-NCSLFNPTPSLSAMVVNHYKLRgNILSYNLGGmGCSAGLISIDLAKHLLHSIPNTY 257
Cdd:TIGR00747 56 FEAAKRAIENAGISKDDIDLIIVaTTTPDHAFPSAACMVQAYLGIK-GIPAFDLSA-ACAGFIYALSVAKQYIESGKYKT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 258 AMVISMENI--TLNWYfgnDRSKLVsncLFRMGGAAILLSNKRWDRrrskyelvDTVRTHKGADDKcfgcitqeedsask 335
Cdd:TIGR00747 134 VLVVGAEKLssTLDWT---DRGTCV---LFGDGAGAVVLGESEDPG--------GIISTHLGADGT-------------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 336 igvtlskelmavAGDALKTNITTLGPlvlPTSEQllfFATLVGRKLFKMKIKPYIPDFKLAFEH----------FCIHAG 405
Cdd:TIGR00747 186 ------------QGEALYLPAGGRPT---SGPSP---FITMEGNEVFKHAVRKMGDVVEETLEAngldpedidwFVPHQA 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225767 406 GRAVLDELEKNLKltewhMEPSRM--TLYRFGNTSSSSLwyELAYSEAK--GRIKKGDRIWQIAFGSGFKCNSSVWR 478
Cdd:TIGR00747 248 NLRIIEALAKRLE-----LDMSQVvkTVHKYGNTSAASI--PLALDELLrtGRIKPGDLLLLVAFGGGLTWGAALVR 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
1-509 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 1079.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 1 MDVEQKKPLIE-SSDRNLPDFKKSVKLKYVKLGYHYLITHGMYLFLSPLVLVIAAQISTFSVTDLRSLWEHLQYNLISVV 79
Cdd:PLN02192 2 SEVNQKTPLIEpSSSRKLPDFKKSVKLKYVKLGYHYLITHGMYLFLSPLVVVIAAQLSTFSIQDLHDLWEHLKFNLISVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 80 VCSMLLVFLMTIYFMTRPRPVYLVNFSCFKPDESRKCTKKIFMDRSKLTGSFTEENLEFQRKILQRSGLGESTYLPEAVL 159
Cdd:PLN02192 82 LCSTLLVFLSTLYFLTRPRPVYLVDFSCYKPDDSRKCTRKIFMDRSKLTGSFTEENLEFQRKILERSGLGESTYLPEAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 160 NVPPNPCMKEARKEAETVMFGAIDELLAKTNVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLGGMGCSAG 239
Cdd:PLN02192 162 NVPPNPCMAEARKEAETVMFGAIDQLLAKTSVKPKDIGILIVNCSLFNPTPSLSAMVINHYKLRGNILSYNLGGMGCSAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 240 LISIDLAKHLLHSIPNTYAMVISMENITLNWYFGNDRSKLVSNCLFRMGGAAILLSNKRWDRRRSKYELVDTVRTHKGAD 319
Cdd:PLN02192 242 LISIDLAKHLLQVHPNSYALVISMENITLNWYFGNDRSMLVSNCLFRMGGAAILLSNKRSDRRRSKYQLVHTVRTHKGAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 320 DKCFGCITQEEDSASKIGVTLSKELMAVAGDALKTNITTLGPLVLPTSEQLLFFATLVGRKLFKMKIKPYIPDFKLAFEH 399
Cdd:PLN02192 322 DKCFACVTQEEDSAGKIGVSLSKDLMAVAGDALKTNITTLGPLVLPMSEQLLFFATLVGKKLFKMKLKPYIPDFKLAFEH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 400 FCIHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGFKCNSSVWRA 479
Cdd:PLN02192 402 FCIHAGGRAVLDELEKNLQLSDWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWKA 481
|
490 500 510
....*....|....*....|....*....|
gi 15225767 480 VRSVNPKKEKNPWMDEIHEFPVEVPKVSTI 509
Cdd:PLN02192 482 LRTVNPAKEKNPWMDEIHEFPVDVPKVSTI 511
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
15-504 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 772.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 15 RNLPDFKKSVKLKYVKLGYHY---LITHGMYLFLSPLVLVIAAQISTFSVTDLRSLW--EHLQYNLISVVVCSMLLVFLM 89
Cdd:PLN02854 24 QRLPDFLQSVKLKYVKLGYGYscnPATILFFLIILPLTIATLVQITGLEFDTVSELWsnQALHLDTATRLTGSAFLLFLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 90 TIYFMTRPRPVYLVNFSCFKPDESRKCTKKIFMDRSKLTGSFTEENLEFQRKILQRSGLGESTYLPEAVLNVPPNPCMKE 169
Cdd:PLN02854 104 GLYWAKRSKPVYLVDFACYKPEDERKISVDSFLTMTEENGSFEDETVQFQRRISTRSGLGDETYLPRGITSRPPNLCMEE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 170 ARKEAETVMFGAIDELLAKTNVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHL 249
Cdd:PLN02854 184 ARAEAEAVMFGALDSLFSKTGVKPRDIGILIVNCSLFNPTPSLSAMIVNHYKLRTDIKSYNLGGMGCSAGLISIDLANDL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 250 LHSIPNTYAMVISMENITLNWYFGNDRSKLVSNCLFRMGGAAILLSNKRWDRRRSKYELVDTVRTHKGADDKCFGCITQE 329
Cdd:PLN02854 264 LKANPNSYAVVVSTENITLNWYFGNDRSMLLCNCIFRMGGAAVLLSNKARDRKRSKYQLVHTVRTHKGADDKNYNCVYQR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 330 EDSASKIGVTLSKELMAVAGDALKTNITTLGPLVLPTSEQLLFFATLVGRKLFKMKIKPYIPDFKLAFEHFCIHAGGRAV 409
Cdd:PLN02854 344 EDDKGTIGVSLARELMAVAGDALKTNITTLGPLVLPLSEQFMFFVTLVRRKLLKAKVKPYIPDFKLAFEHFCIHAGGRAV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 410 LDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGFKCNSSVWRAVRSVNPKKEK 489
Cdd:PLN02854 424 LDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWYELAYTEAKGRVSAGDRVWQIAFGSGFKCNSAVWKALREIPTGEST 503
|
490
....*....|....*.
gi 15225767 490 -NPWMDEIHEFPVEVP 504
Cdd:PLN02854 504 gNPWADSIDRYPVKVP 519
|
|
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
15-503 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 748.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 15 RNLPDFKKSVKLKYVKLGYHYLITHGMYLFLSPLVLVIAAQISTFSVTDLRSLWEHLQYNLISVVVCSMLLVFLMTIYFM 94
Cdd:PLN02377 13 RMLPDFLQSVNLKYVKLGYHYLISNLLTLCFIPLIIIISIEASQMNPDDLRQLWIHLQYNLVSIIICSAFLVFGLTVYIM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 95 TRPRPVYLVNFSCFKPDESRKCTKKIFMDRSKLTGSFTEENLEFQRKILQRSGLGESTYLPEAVLNVPPNPCMKEARKEA 174
Cdd:PLN02377 93 TRPRPVYLVDYSCYRAPDHLKAPFARFMEHSRLTGDFDDSSLEFQRKILERSGLGEDTYVPEAMHYIPPRPSMAAAREEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 175 ETVMFGAIDELLAKTNVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLHSIP 254
Cdd:PLN02377 173 EQVMFGALDNLFANTNVNPKDIGILVVNCSLFNPTPSLSAMIVNKYKLRGNIRSFNLGGMGCSAGVIAVDLAKDMLQVHR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 255 NTYAMVISMENITLNWYFGNDRSKLVSNCLFRMGGAAILLSNKRWDRRRSKYELVDTVRTHKGADDKCFGCITQEEDSAS 334
Cdd:PLN02377 253 NTYAVVVSTENITQNWYFGNKKSMLIPNCLFRVGGSAVLLSNKSRDKRRSKYKLVHVVRTHRGADDKAFRCVYQEQDDAG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 335 KIGVTLSKELMAVAGDALKTNITTLGPLVLPTSEQLLFFATLVGRKLFKMKIKPYIPDFKLAFEHFCIHAGGRAVLDELE 414
Cdd:PLN02377 333 KTGVSLSKDLMAIAGEALKTNITTLGPLVLPISEQLLFFATLVVKKLFNKKMKPYIPDFKLAFDHFCIHAGGRAVIDELE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 415 KNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGFKCNSSVWRAVRSVNPKKeKNPWMD 494
Cdd:PLN02377 413 KNLQLLPVHVEASRMTLHRFGNTSSSSIWYELAYIEAKGRMRKGNRVWQIAFGSGFKCNSAVWEALRHVKPSN-NSPWED 491
|
....*....
gi 15225767 495 EIHEFPVEV 503
Cdd:PLN02377 492 CIDKYPVKL 500
|
|
| PLN02932 |
PLN02932 |
3-ketoacyl-CoA synthase |
33-503 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 178520 Cd Length: 478 Bit Score: 610.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 33 YHYLITHGMYLFLSPLVLVIAAQISTFSVTDLRSLWEHLQYNLISVVVCSMLLVFLMTIYFMTRPRPVYLVNFSCFKPDE 112
Cdd:PLN02932 1 FNYLMAHRFKLCFLPLMVGIAMEASRLSTQDLQNFYLYLQNNLTSLTMFFLYLALGSTLYLMTRPKPVYLVDFSCYLPPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 113 SRKCTKKIFMDRSKLT---GSFTEEN---LEFQRKILQRSGLGESTYLPEAVLNVPPNPCMKEARKEAETVMFGAIDELL 186
Cdd:PLN02932 81 HLKASIQTIMGHVRRVreaGAWKQESdylMDFCEKILERSGLGQETYIPEGLQCLPLQQNLAVSRKETEEVIIGAVDNLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 187 AKTNVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLHSIPNTYAMVISMENI 266
Cdd:PLN02932 161 RNTGISPSDIGILVVNSSTFNPTPSLSSILVNKFKLRDNIKSLNLGGMGCSAGVIAIDAAKSLLQVHRNTYALVVSTENI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 267 TLNWYFGNDRSKLVSNCLFRMGGAAILLSNKRWDRRRSKYELVDTVRTHKGADDKCFGCITQEEDSASKIGVTLSKELMA 346
Cdd:PLN02932 241 TQNLYLGNNKSMLVTNCLFRIGGAAILLSNRSRDRKRAKYELVHTVRVHTGADDRSYECATQEEDEDGIVGVSLSKNLPM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 347 VAGDALKTNITTLGPLVLPTSEQLLFFATLVGRKLFKMKIKPYIPDFKLAFEHFCIHAGGRAVLDELEKNLKLTEWHMEP 426
Cdd:PLN02932 321 VAARTLKINIATLGPLVLPLSEKFHFFVRFVKKKFFNPKLKHYIPDFKLAFEHFCIHAGGRALIDEMEKNLHLTPLDVEA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225767 427 SRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGFKCNSSVWRAVRSVNPKKeKNPWMDEIHEFPVEV 503
Cdd:PLN02932 401 SRMTLHRFGNTSSSSIWYELAYTEAKGRMKKGDRIWQIALGSGFKCNSSVWVALRNVKPSA-NNPWEDCLHKYPVEI 476
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
92-381 |
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: 564.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 92 YFMTRPRPVYLVNFSCFKPDESRKCTKKIFMDRSKLTGSFTEENLEFQRKILQRSGLGESTYLPEAVLNVPPNPCMKEAR 171
Cdd:pfam08392 1 YLARRPRPVYLVDYSCYKPPDDRKVSTETFMEHIQRNGHLDLESLDFQRKILERSGLGEETYLPRAVLEGPPDPTLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 172 KEAETVMFGAIDELLAKTNVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLH 251
Cdd:pfam08392 81 EEAEEVIFGAVDDLFAKTGVSPRDIDILVVNCSLFNPTPSLSAMIVNRYKLRSDIKSYNLSGMGCSAGLISIDLAKNLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 252 SIPNTYAMVISMENITLNWYFGNDRSKLVSNCLFRMGGAAILLSNKRWDRRRSKYELVDTVRTHKGADDKCFGCITQEED 331
Cdd:pfam08392 161 VHPNTYALVVSTENITPNWYFGNDRSMLLPNCLFRMGGAAVLLSNRPADRRRAKYELVHTVRTHKGADDRAYNCVYQEED 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15225767 332 SASKIGVTLSKELMAVAGDALKTNITTLGPLVLPTSEQLLFFATLVGRKL 381
Cdd:pfam08392 241 EDGKVGVSLSKDLMKVAGRALKTNITTLGPLVLPLSEQLRFAATLLARKL 290
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
48-503 |
0e+00 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 543.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 48 LVLVIAAQISTFSVTDLRslWEHLQYNLISVVVCSMLLVFLMTIYFMTRPRPVYLVNFSCFKPDESRKCTKKIFMDRSKL 127
Cdd:PLN00415 10 LLLLILILLSLFELDLLH--FHHDFFSPFPVKIGLLLISIFFYAYSTTRSKPVYLVDFSCHQPTDSCKISSETFFNMAKG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 128 TGSFTEENLEFQRKILQRSGLGESTYLPEAVLNVPPNPCMKEARKEAETVMFGAIDELLAKTNVNPKDIGILIVNCSLFN 207
Cdd:PLN00415 88 AQLYTEETIQFMTRILNRSGLGDDTYSPRCMLTSPPTPSMYEARHESELVIFGALNSLFKKTGIEPREVGIFIVNCSLFN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 208 PTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLHSIPNTYAMVISMENITLNWYFGNDRSKLVSNCLFRM 287
Cdd:PLN00415 168 PNPSLSSMIVNRYKLKTDVKTYNLSGMGCSAGAISVDLATNLLKANPNTYAVIVSTENMTLSMYRGNDRSMLVPNCLFRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 288 GGAAILLSNKRWDRRRSKYELVDTVRTHKGADDKCFGCITQEEDSASKIGVTLSKELMAVAGDALKTNITTLGPLVLPTS 367
Cdd:PLN00415 248 GGAAVMLSNRSQDRVRSKYELTHIVRTHKGSSDKHYTCAEQKEDSKGIVGVALSKELTVVAGDTLKTNLTALGPLVLPLS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 368 EQLLFFATLVGRKLFKMKIKPYIPDFKLAFEHFCIHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELA 447
Cdd:PLN00415 328 EKLRFILFLVKSKLFRLKVSPYVPDFKLCFKHFCIHAGGRALLDAVEKGLGLSEFDLEPSRMTLHRFGNTSSSSLWYELA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15225767 448 YSEAKGRIKKGDRIWQIAFGSGFKCNSSVWRAVRSVnPKKEK---NPWMDEIHEFPVEV 503
Cdd:PLN00415 408 YVEAKCRVKRGDRVWQLAFGSGFKCNSIVWRALRTI-PANESlvgNPWGDSVHKYPVHV 465
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
77-477 |
1.28e-141 |
|
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: 411.62 E-value: 1.28e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 77 SVVVCSMLLVFLMTIYFMTRPRPVYLVNFSCFKPDESRKCTKKIFmdrskltgsfteENLEFQRKILQRSGlGESTYLP- 155
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLC------------AKTGIETRYLVLPG-GEETYAPr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 156 ---EAVLNVPPNPCMKEARKEAETVMFGAIDELLaktnVNPKDIGILIVNCSLFNPTPSLSAMVVNHYKLRGNILSYNLG 232
Cdd:cd00831 68 pemSPSLDERNDIALEEARELAEEAARGALDEAG----LRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 233 GMGCSAGLISIDLAKHLLHSIPNTYAMVISMENITLnWYFGND-RSKLVSNCLFRMGGAAILLSNKRWDRR--RSKYELV 309
Cdd:cd00831 144 GMGCSAGAIALDLAKDLLEANPGARVLVVSTELCSL-WYRGPDhRSMLVGNALFGDGAAAVLLSNDPRDRRreRPLFELV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 310 DTVRTHKgaddkcfgcitqeEDSASKIGVTLSKELMAVagdalktnitTLGPLVLPTSEQLLFFatlVGRKLFKmkiKPY 389
Cdd:cd00831 223 RAASTLL-------------PDSEDAMGWHLGEEGLTF----------VLSRDVPRLVEKNLER---VLRKLLA---RLG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 390 IPDFKLAFEHFCIHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSG 469
Cdd:cd00831 274 IGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPG 353
|
....*...
gi 15225767 470 FKCNSSVW 477
Cdd:cd00831 354 FTCESAVW 361
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
181-470 |
8.13e-35 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 133.73 E-value: 8.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 181 AIDELLAKTNVNPKDIGILI-VNCSLFNpTPSLSAMVVNHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLHSIPNTYAM 259
Cdd:COG3424 84 AARRALDKAGLDPEDIDHLVtVSCTGFA-APGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFLRADPDAVVL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 260 VISMENITLNWYFGND-RSKLVSNCLFRMGGAAILLSNKrwDRRRSKYELVDTvRTHkgaddkcfgCITQEED------S 332
Cdd:COG3424 163 VVCVELCSLTFQRDDDsKDNLVANALFGDGAAAVVVSGD--PRPGPGPRILAF-RSY---------LIPDTEDvmgwdvG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 333 ASKIGVTLSKELMAVAGDALKTNITTLgplvlptseqllffatLVGRKLFKMKIkpyipdfklafEHFCIHAGGRAVLDE 412
Cdd:COG3424 231 DTGFRMVLSPEVPDLIAEHLAPAVEPL----------------LARHGLTIEDI-----------DHWAVHPGGPKVLDA 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15225767 413 LEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGF 470
Cdd:COG3424 284 VEEALGLPPEALAHSREVLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGF 341
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
181-470 |
2.26e-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: 80.17 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 181 AIDELLAKTNVNPKDIGILIVNC-SLFNPTPSlSAMVVNHYKLRGNILSYNLGGmGCSAGLISIDLAKHLLHSIPNTYAM 259
Cdd:cd00827 55 AARRALERAGIDPDDIGLLIVATeSPIDKGKS-AATYLAELLGLTNAEAFDLKQ-ACYGGTAALQLAANLVESGPWRYAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 260 VIS--------MENITLNWYFGnDrsklvsnclfrmGGAAILLSNkrwDRRRSKYELVDTVRTHKGADDKCF-----GCI 326
Cdd:cd00827 133 VVAsdiasyllDEGSALEPTLG-D------------GAAAMLVSR---NPGILAAGIVSTHSTSDPGYDFSPypvmdGGY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 327 TQEEDSASKIGVTLSKELMAVAGDALKTnittlgplvlptseqllfFATLVGRKLFKMKIKPYIPDFklafehFCIHAGG 406
Cdd:cd00827 197 PKPCKLAYAIRLTAEPAGRAVFEAAHKL------------------IAKVVRKALDRAGLSEDIDYF------VPHQPNG 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225767 407 RAVLDELEKNLKLTEWHMEPSRMTLYRF-GNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGF 470
Cdd:cd00827 253 KKILEAVAKKLGGPPEKASQTRWILLRRvGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGF 317
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
181-478 |
1.45e-15 |
|
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: 77.46 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 181 AIDELLAKTNVNPKDIGILIVN-CSLFNPTPSLSAMVvnHYKLrG--NILSYNLGGmGCSAGLISIDLAKHLLHSIPNTY 257
Cdd:COG0332 58 AARKALEAAGIDPEDIDLIIVAtVTPDYLFPSTACLV--QHKL-GakNAAAFDINA-ACSGFVYALSVAAALIRSGQAKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 258 AMVISMENIT--LNWyfgNDRSklvSNCLFRMGGAAILLSnkrwdRRRSKYELVDTVrthkgaddkcFGCITQEEDsask 335
Cdd:COG0332 134 VLVVGAETLSriVDW---TDRS---TCVLFGDGAGAVVLE-----ASEEGPGILGSV----------LGSDGSGAD---- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 336 igvtlskeLMAVAGDALKTNITTLgplvlptsEQLLFFATLVGRKLFKMKIKpYIPDF--------KLAFE---HFCIHA 404
Cdd:COG0332 189 --------LLVVPAGGSRNPPSPV--------DEGDHYLRMDGREVFKFAVR-NLPEVirealekaGLTLDdidWFIPHQ 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225767 405 GGRAVLDELEKNLKLtewhmEPSR--MTLYRFGNTSSSSLwyELAYSEA--KGRIKKGDRIWQIAFGSGFKCNSSVWR 478
Cdd:COG0332 252 ANLRIIEAVAKRLGL-----PEEKvvVNIDRYGNTSAASI--PLALDEAlrEGRIKPGDLVLLAGFGAGLTWGAAVLR 322
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
181-477 |
9.33e-14 |
|
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: 72.19 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 181 AIDELLAKTNVNPKDIGILIV-NCSLFNPTPSLSAMVvnHYKLR-GNILSYNLGGmGCSAGLISIDLAKHLLHSIPNTYA 258
Cdd:cd00830 57 AAKKALEDAGIDADDIDLIIVaTSTPDYLFPATACLV--QARLGaKNAAAFDINA-ACSGFLYGLSTAAGLIRSGGAKNV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 259 MVISMENIT--LNWyfgNDRSKLVsncLFRMGGAAILLSnkrwdRRRSKYELVDTVRthkGADDKCFGCITqeedsASKI 336
Cdd:cd00830 134 LVVGAETLSriLDW---TDRSTAV---LFGDGAGAVVLE-----ATEEDPGILDSVL---GSDGSGADLLT-----IPAG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 337 GVTLSKELMAVAGDALKTNittlgplvlptseqllffatlvGRKLFKMKIKpYIPDF--KLAFE---------HFCIHAG 405
Cdd:cd00830 195 GSRSPFEDAEGGDPYLVMD----------------------GREVFKFAVR-LMPESieEALEKagltpddidWFVPHQA 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225767 406 GRAVLDELEKNLKLtewhmEPSR--MTLYRFGNTSSSSLwyELAYSEA--KGRIKKGDRIWQIAFGSGFKCNSSVW 477
Cdd:cd00830 252 NLRIIEAVAKRLGL-----PEEKvvVNLDRYGNTSAASI--PLALDEAieEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
179-478 |
1.52e-11 |
|
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: 65.48 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 179 FGAIDELLAKTNVNPKDIGILIV-NCSLFNPTPSLSAMVVNHYKLRgNILSYNLGGmGCSAGLISIDLAKHLLHSIPNTY 257
Cdd:TIGR00747 56 FEAAKRAIENAGISKDDIDLIIVaTTTPDHAFPSAACMVQAYLGIK-GIPAFDLSA-ACAGFIYALSVAKQYIESGKYKT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 258 AMVISMENI--TLNWYfgnDRSKLVsncLFRMGGAAILLSNKRWDRrrskyelvDTVRTHKGADDKcfgcitqeedsask 335
Cdd:TIGR00747 134 VLVVGAEKLssTLDWT---DRGTCV---LFGDGAGAVVLGESEDPG--------GIISTHLGADGT-------------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 336 igvtlskelmavAGDALKTNITTLGPlvlPTSEQllfFATLVGRKLFKMKIKPYIPDFKLAFEH----------FCIHAG 405
Cdd:TIGR00747 186 ------------QGEALYLPAGGRPT---SGPSP---FITMEGNEVFKHAVRKMGDVVEETLEAngldpedidwFVPHQA 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225767 406 GRAVLDELEKNLKltewhMEPSRM--TLYRFGNTSSSSLwyELAYSEAK--GRIKKGDRIWQIAFGSGFKCNSSVWR 478
Cdd:TIGR00747 248 NLRIIEALAKRLE-----LDMSQVvkTVHKYGNTSAASI--PLALDELLrtGRIKPGDLLLLVAFGGGLTWGAALVR 317
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
399-478 |
1.56e-10 |
|
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: 57.51 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 399 HFCIHAGGRAVLDELEKNLKLTEwhmEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRIWQIAFGSGFKCNSSVWR 478
Cdd:pfam08541 13 WFVPHQANLRIIDAVAKRLGLPP---EKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAGLTWGAALLR 89
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
181-470 |
4.84e-09 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 57.95 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 181 AIDELLAKTNVNPKDIGILIVN-CSLFNPTPSLSAMVVNHYKLRgNILSYNLGGmGCSAGLISIDLAKHLLHSIPNTYAM 259
Cdd:PRK12879 60 AAERALARAGLDAEDIDLIIVAtTTPDYLFPSTASQVQARLGIP-NAAAFDINA-ACAGFLYGLETANGLITSGLYKKVL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 260 VISMENIT--LNWyfgNDRSKLVsncLFRMGGAAILLSnkrwdRRRSKYELVDTVRTHKGAddkcfgcitqeedsaskig 337
Cdd:PRK12879 138 VIGAERLSkvTDY---TDRTTCI---LFGDGAGAVVLE-----ATENEPGFIDYVLGTDGD------------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 338 vtlskelmavAGDALKtnITTLGPLVLPTSEQLLFFATLVGRKLFKMKIKPyIPD-FKLAFE----------HFCIHAGG 406
Cdd:PRK12879 188 ----------GGDILY--RTGLGTTMDRDALSGDGYIVQNGREVFKWAVRT-MPKgARQVLEkagltkddidWVIPHQAN 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225767 407 RAVLDELEKNLKLTewhMEPSRMTLYRFGNTSSSSLwyELAYSEA--KGRIKKGDRIWQIAFGSGF 470
Cdd:PRK12879 255 LRIIESLCEKLGIP---MEKTLVSVEYYGNTSAATI--PLALDLAleQGKIKPGDTLLLYGFGAGL 315
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
234-469 |
6.51e-09 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 57.79 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 234 MGCSAGLISIDLAKHLLHSIPNTYAMVISMENITLNWYFGN-DRS-KLVSNCLFRMG-GAAILLSNKRWDRRRSKYELVD 310
Cdd:PLN03169 166 LGCSGGVAGLRVAKDIAENNPGSRVLLTTSETTILGFRPPSpDRPyDLVGAALFGDGaAAVIIGADPIPVSESPFFELHT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 311 TVR-----THKGADdkcfGCITQEedsasKIGVTLSKELMAVagdaLKTNITTlgplvlptseqllFFATLVGRKLFKMK 385
Cdd:PLN03169 246 AIQqflpgTEKTID----GRLTEE-----GINFKLGRELPQK----IEDNIEG-------------FCKKLMKKAGLVEK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 386 ikpyipDFKLAFehFCIHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAY-SEAKGRIKKGDRIWQI 464
Cdd:PLN03169 300 ------DYNDLF--WAVHPGGPAILNRLEKKLKLAPEKLECSRRALMDYGNVSSNTIVYVLEYmREELKKKGEEDEEWGL 371
|
....*..
gi 15225767 465 --AFGSG 469
Cdd:PLN03169 372 ilAFGPG 378
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
402-480 |
1.99e-06 |
|
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: 47.45 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 402 IHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYELAY---SEAKGRIKKGDRI--WQI--AFGSGFKCNS 474
Cdd:pfam02797 65 VHPGGPAILDRVETKLGLEPEKLEASRRALMDYGNVSSATVLFILDEmrkKSLKKGLATTGEGldWGVllAFGPGLTFET 144
|
....*.
gi 15225767 475 SVWRAV 480
Cdd:pfam02797 145 VVLRSV 150
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
391-446 |
4.75e-06 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 48.88 E-value: 4.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15225767 391 PDFKLAFehFCIHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYEL 446
Cdd:PLN03168 292 PDWNEMF--WAVHPGGPAILDQVEAKLKLTKDKMQGSRDILSEFGNMSSASVLFVL 345
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
410-470 |
9.59e-06 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 47.38 E-value: 9.59e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225767 410 LDELEKNLKLTewhMEPSRMTLYRFGNTSSSSLwyELAYSEA--KGRIKKGDRIWQIAFGSGF 470
Cdd:PRK09352 252 IDATAKKLGLP---MEKVVVTVDKYGNTSAASI--PLALDEAvrDGRIKRGDLVLLEGFGGGL 309
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
398-478 |
1.67e-03 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 40.88 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 398 EHFCIHAGGRAVLDELEKNLkltewHMEPSRM--TLYRFGNTSSSSLwyELAYSEA--KGRIKKGDRIWQIAFGSGFKCN 473
Cdd:PLN02326 301 DWLLLHQANQRIIDAVAQRL-----GIPPEKVisNLANYGNTSAASI--PLALDEAvrSGKVKKGDVIATAGFGAGLTWG 373
|
....*
gi 15225767 474 SSVWR 478
Cdd:PLN02326 374 SAIVR 378
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
153-469 |
3.79e-03 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 39.70 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 153 YLPEAVLNVPPNPCMK-----EARKEAETVMFGAIDELLAKTNV----NPKDIGILIVNCSLFN-PTPSLSAMVVNHYKL 222
Cdd:PLN03170 75 HLTEEYLAENPNMCAYmapslDARQDIVVVEVPKLGKAAAQKAIkewgQPKSKITHLVFCTTSGvDMPGADYQLTKMLGL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 223 RGNILSYNLGGMGCSAGLISIDLAKHLLHSIPNTYAMVISMEnITLNWYFGNDRSKL---VSNCLFRMGGAAILLSNKRW 299
Cdd:PLN03170 155 RPSVNRLMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSE-ITAVTFRGPSESHLdsmVGQALFGDGAAAVIVGADPD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 300 DR-RRSKYELVDTVRT----HKGADDKCFGCITQEEDSASKIGVTLSKELMAVAGDALKtnittlgPLVLPTSEQLLFFA 374
Cdd:PLN03170 234 ERvERPLFQLVSASQTilpdSEGAIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFK-------PLGITDYNSIFWVA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225767 375 tlvgrklfkmkikpyipdfklafehfciHAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYEL----AYSE 450
Cdd:PLN03170 307 ----------------------------HPGGPAILDQVEAKVGLEKERMRATRHVLSEYGNMSSACVLFILdemrKRSA 358
|
330 340
....*....|....*....|
gi 15225767 451 AKGRIKKGDRI-WQIAFGSG 469
Cdd:PLN03170 359 EDGQATTGEGFdWGVLFGFG 378
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
403-469 |
5.62e-03 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 39.27 E-value: 5.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225767 403 HAGGRAVLDELEKNLKLTEWHMEPSRMTLYRFGNTSSSSLWYEL------AYSEAKGRIKKGDRiWQIAFGSG 469
Cdd:PLN03172 303 HPGGPAILDQVEIKLDLKEEKLRATRHVLSDYGNMSSACVLFILdemrkkSIEEGKGSTGEGLE-WGVLFGFG 374
|
|
| |
