|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
1-388 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 722.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 1 MVSVSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKEN 80
Cdd:PLN03173 1 MVTVDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 81 PNVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMY 160
Cdd:PLN03173 81 PSVCEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMV 240
Cdd:PLN03173 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGVEKPLFELV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 241 WTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALK 320
Cdd:PLN03173 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CGK_A 321 PEKMNATREVLSEYGNMSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVLRSVA 388
Cdd:PLN03173 321 PEKLRATRHVLSEYGNMSSACVLFILDEMRKKSAEDGLKSTGEGLEWGVLFGFGPGLTVETVVLHSVA 388
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
16-384 |
1.93e-172 |
|
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: 485.19 E-value: 1.93e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 16 PATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLT--EEILKENPNvceyMAPSLDA 93
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPE----MSPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 94 RQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRL 173
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 174 AKDLAENNKGARVLVVCSEVTAVTFRGPSdtHLDSLVGQALFGDGAAALIVGSDPVPE-IEKPIFEMVWTAQTIAPDSEG 252
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRrRERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 253 AIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPL--GISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMNATREV 330
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
1CGK_A 331 LSEYGNMSSACVLFILDEMRKKSTQnglkttgEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00831 315 LRRYGNMSSSSVLYVLAYMEAKGRV-------KRGDRGLLIAFGPGFTCESAVW 361
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
4-228 |
1.89e-148 |
|
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: 419.26 E-value: 1.89e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 4 VSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKENPNV 83
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 84 CEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQG 163
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1CGK_A 164 CFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDP 228
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
16-385 |
4.06e-100 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 300.90 E-value: 4.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 16 PATILAIGTANPANCVEQSTYPDFYFKITNSEHKTelKEKFQRMCDKSMIKRRYMYLTEEILKENPnvceymapSLDARQ 95
Cdd:COG3424 1 SARILSIATAVPPHRYTQEEIAEFAAELFGLDERD--RRRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 96 DMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAK 175
Cdd:COG3424 71 ALYIEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 176 DLAENNKGARVLVVCSEVTAVTFRgPSDTHLDSLVGQALFGDGAAALIVGSDPVPEiekPIFEMVWTAQTIAPDSEGAID 255
Cdd:COG3424 151 DFLRADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPG---PGPRILAFRSYLIPDTEDVMG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 256 GHLREAGLTFHLLKDVPGIVSKNItKALVEAF---EPLGISDYNsiFWIAHPGGPAILDQVEQKLALKPEKMNATREVLS 332
Cdd:COG3424 227 WDVGDTGFRMVLSPEVPDLIAEHL-APAVEPLlarHGLTIEDID--HWAVHPGGPKVLDAVEEALGLPPEALAHSREVLR 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
1CGK_A 333 EYGNMSSACVLFILDEMRKKSTQnglkttGEGlEWGVLFGFGPGLTIETVVLR 385
Cdd:COG3424 304 EYGNMSSATVLFVLERLLEEGAP------APG-ERGLAMAFGPGFTAELVLLR 349
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
105-385 |
1.24e-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: 70.88 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 105 LGKEAAVKAIKEWGQPKSKITHLIVCTTS-GVDMPGADYQLTKLLGLRPyvKRYMMYQQGCFAGGTVLRLAKDLAENNKG 183
Cdd:TIGR00747 54 MGFEAAKRAIENAGISKDDIDLIIVATTTpDHAFPSAACMVQAYLGIKG--IPAFDLSAACAGFIYALSVAKQYIESGKY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 184 ARVLVVCSEVTAVTF----RGPSdthldslvgqALFGDGAAALIVGSDPVPE--IEKPIF------EMVWTAQTIAPDSE 251
Cdd:TIGR00747 132 KTVLVVGAEKLSSTLdwtdRGTC----------VLFGDGAGAVVLGESEDPGgiISTHLGadgtqgEALYLPAGGRPTSG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 252 GAidGHLREAGltfhllKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMNATrevL 331
Cdd:TIGR00747 202 PS--PFITMEG------NEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKT---V 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
1CGK_A 332 SEYGNMSSACVLFILDEmrkkstqngLKTTGEgLEWG---VLFGFGPGLTIETVVLR 385
Cdd:TIGR00747 271 HKYGNTSAASIPLALDE---------LLRTGR-IKPGdllLLVAFGGGLTWGAALVR 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
1-388 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 722.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 1 MVSVSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKEN 80
Cdd:PLN03173 1 MVTVDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 81 PNVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMY 160
Cdd:PLN03173 81 PSVCEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMV 240
Cdd:PLN03173 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGVEKPLFELV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 241 WTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALK 320
Cdd:PLN03173 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CGK_A 321 PEKMNATREVLSEYGNMSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVLRSVA 388
Cdd:PLN03173 321 PEKLRATRHVLSEYGNMSSACVLFILDEMRKKSAEDGLKSTGEGLEWGVLFGFGPGLTVETVVLHSVA 388
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
1-389 |
0e+00 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 689.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 1 MVSVSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKEN 80
Cdd:PLN03172 1 APSIAEIRKAQRAEGPATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 81 PNVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMY 160
Cdd:PLN03172 81 PNMCAYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 161 QQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMV 240
Cdd:PLN03172 161 QQGCFAGGTVLRLAKDLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKIERPLFEIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 241 WTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALK 320
Cdd:PLN03172 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1CGK_A 321 PEKMNATREVLSEYGNMSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVLRSVAI 389
Cdd:PLN03172 321 EEKLRATRHVLSDYGNMSSACVLFILDEMRKKSIEEGKGSTGEGLEWGVLFGFGPGLTVETVVLHSVPA 389
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
2-389 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 669.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 2 VSVSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKENP 81
Cdd:PLN03170 6 VTVEEVRKAQRATGPATVLAIGTATPANCVHQADYPDYYFRITKSEHMTELKEKFKRMCDKSQIRKRYMHLTEEYLAENP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 82 NVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQ 161
Cdd:PLN03170 86 NMCAYMAPSLDARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNRLMMYQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 162 QGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMVW 241
Cdd:PLN03170 166 QGCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSESHLDSMVGQALFGDGAAAVIVGADPDERVERPLFQLVS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 242 TAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKP 321
Cdd:PLN03170 246 ASQTILPDSEGAIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAKVGLEK 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CGK_A 322 EKMNATREVLSEYGNMSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVLRSVAI 389
Cdd:PLN03170 326 ERMRATRHVLSEYGNMSSACVLFILDEMRKRSAEDGQATTGEGFDWGVLFGFGPGLTVETVVLHSVPI 393
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
8-389 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 561.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 8 RKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKENPNVCEYM 87
Cdd:PLN03168 7 RGQPRAEGPACVLGIGTAVPPAEFLQSEYPDFFFNITNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVLKANPGICTYM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 88 APSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAG 167
Cdd:PLN03168 87 EPSLNVRHDIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGADHALAKLLGLKPTVKRVMMYQTGCFGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 168 GTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMVWTAQTIA 247
Cdd:PLN03168 167 ASVLRVAKDLAENNKGARVLAVASEVTAVTYRAPSENHLDGLVGSALFGDGAGVYVVGSDPKPEVEKALFEVHWAGETIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 248 PDSEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMNAT 327
Cdd:PLN03168 247 PESDGAIDGHLTEAGLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQGS 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
1CGK_A 328 REVLSEYGNMSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVLRSVAI 389
Cdd:PLN03168 327 RDILSEFGNMSSASVLFVLDQIRQRSVKMGASTLGEGSEFGFFIGFGPGLTLEVLVLRAAAN 388
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
16-384 |
1.93e-172 |
|
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: 485.19 E-value: 1.93e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 16 PATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLT--EEILKENPNvceyMAPSLDA 93
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPE----MSPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 94 RQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRL 173
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 174 AKDLAENNKGARVLVVCSEVTAVTFRGPSdtHLDSLVGQALFGDGAAALIVGSDPVPE-IEKPIFEMVWTAQTIAPDSEG 252
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRrRERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 253 AIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPL--GISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMNATREV 330
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
1CGK_A 331 LSEYGNMSSACVLFILDEMRKKSTQnglkttgEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00831 315 LRRYGNMSSSSVLYVLAYMEAKGRV-------KRGDRGLLIAFGPGFTCESAVW 361
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
3-384 |
1.85e-166 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 471.80 E-value: 1.85e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 3 SVSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKENPN 82
Cdd:PLN03171 9 NLGEICRAQRADGLAAVLAIGTANPANCVPQDEFPDFYFRATKSDHLTALKDKFKRICQELGVQKRYLHHTEELLSAHPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 83 VCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQ 162
Cdd:PLN03171 89 FLDHDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAHIPGVDFRLVPLLGLRPSVRRTMLHLN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 163 GCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVpEIEKPIFEMVWT 242
Cdd:PLN03171 169 GCFAGAAALRLAKDLAENNRGARVLVVAAEITLLLFNGPDEGCFQTLLNQGLFGDGAAAVIVGADAD-AAERPLFEIVSA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 243 AQTIAPDSEGAIDGHLREAGLTFHL-LKDVPGIVSKNITKALVEAFEPL----GISDYNSIFWIAHPGGPAILDQVEQKL 317
Cdd:PLN03171 248 AQAIIPESDDAINMHFTEGGLDGNIgTRQVPGLIGDNIERCLLDAFAPLlggdGGAEWNDLFWAVHPGSSAILDQVDAAL 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CGK_A 318 ALKPEKMNATREVLSEYGNMSSACVLFILDEMRKKSTQNglKTTGEGLEWGVLFGFGPGLTIETVVL 384
Cdd:PLN03171 328 GLEPEKLAASRRVLSDYGNMFGATVIFALDELRRQMEEA--AAAGAWPELGVMMAFGPGLTVDAMLL 392
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
4-228 |
1.89e-148 |
|
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: 419.26 E-value: 1.89e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 4 VSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKENPNV 83
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 84 CEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQG 163
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1CGK_A 164 CFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDP 228
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
15-387 |
2.26e-129 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 377.12 E-value: 2.26e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 15 GPATILAIGTANPANCVEQSTYPDFYFKITNSEhKTELKEKFQRMCDKSMIKRRYMYLTEEILKENPNVCEYMAPSLDAR 94
Cdd:PLN03169 20 GKATILALGKAFPSQLVPQEYLVDGYFRDTKCD-DPALKEKLERLCKTTTVKTRYVVMSKEILDKYPELATEGTPTIKQR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 95 QDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLA 174
Cdd:PLN03169 99 LDIANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEARLPGGDLYLAKQLGLSPDVQRVMLYFLGCSGGVAGLRVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 175 KDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMVWTAQTIAPDSEGAI 254
Cdd:PLN03169 179 KDIAENNPGSRVLLTTSETTILGFRPPSPDRPYDLVGAALFGDGAAAVIIGADPIPVSESPFFELHTAIQQFLPGTEKTI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 255 DGHLREAGLTFHLLKDVPGIVSKNItkalvEAF-------EPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMNAT 327
Cdd:PLN03169 259 DGRLTEEGINFKLGRELPQKIEDNI-----EGFckklmkkAGLVEKDYNDLFWAVHPGGPAILNRLEKKLKLAPEKLECS 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 328 REVLSEYGNMSSACVLFILDEMRKKStqngLKTTGEGLEWGVLFGFGPGLTIETVVLRSV 387
Cdd:PLN03169 334 RRALMDYGNVSSNTIVYVLEYMREEL----KKKGEEDEEWGLILAFGPGITFEGILARNL 389
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
16-385 |
4.06e-100 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 300.90 E-value: 4.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 16 PATILAIGTANPANCVEQSTYPDFYFKITNSEHKTelKEKFQRMCDKSMIKRRYMYLTEEILKENPnvceymapSLDARQ 95
Cdd:COG3424 1 SARILSIATAVPPHRYTQEEIAEFAAELFGLDERD--RRRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 96 DMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAK 175
Cdd:COG3424 71 ALYIEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 176 DLAENNKGARVLVVCSEVTAVTFRgPSDTHLDSLVGQALFGDGAAALIVGSDPVPEiekPIFEMVWTAQTIAPDSEGAID 255
Cdd:COG3424 151 DFLRADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPG---PGPRILAFRSYLIPDTEDVMG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 256 GHLREAGLTFHLLKDVPGIVSKNItKALVEAF---EPLGISDYNsiFWIAHPGGPAILDQVEQKLALKPEKMNATREVLS 332
Cdd:COG3424 227 WDVGDTGFRMVLSPEVPDLIAEHL-APAVEPLlarHGLTIEDID--HWAVHPGGPKVLDAVEEALGLPPEALAHSREVLR 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
1CGK_A 333 EYGNMSSACVLFILDEMRKKSTQnglkttGEGlEWGVLFGFGPGLTIETVVLR 385
Cdd:COG3424 304 EYGNMSSATVLFVLERLLEEGAP------APG-ERGLAMAFGPGFTAELVLLR 349
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
238-387 |
9.68e-86 |
|
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: 256.99 E-value: 9.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 238 EMVWTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKL 317
Cdd:pfam02797 1 ELVSAAQTFLPNTDGVIDGHLTEEGLTFHLGRDVPQKIEENIEEFLKKAFEPLGISEWNSLFWIVHPGGPAILDRVETKL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 318 ALKPEKMNATREVLSEYGNMSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVLRSV 387
Cdd:pfam02797 81 GLEPEKLEASRRALMDYGNVSSATVLFILDEMRKKSLKKGLATTGEGLDWGVLLAFGPGLTFETVVLRSV 150
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
102-384 |
4.60e-56 |
|
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: 184.57 E-value: 4.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 102 VPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVD-MPGADYQLTKLLGLrPYVKRYMMYQqGCFAGGTVLRLAKDLAEN 180
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGeFSGAAGQLAYHLGI-SGGPAYSVNQ-ACATGLTALALAVQQVQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 181 NKGARVLVVCSEVtavtfrgpsdthldslvgqALFGDGAAALIVGSDP--VPEIEKPIFEMVWTAQTIAPDSEgaidghl 258
Cdd:cd00327 85 GKADIVLAGGSEE-------------------FVFGDGAAAAVVESEEhaLRRGAHPQAEIVSTAATFDGASM------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 259 reagltfhllkdVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMN--ATREVLSEYGN 336
Cdd:cd00327 139 ------------VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRspAVSATLIMTGH 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
1CGK_A 337 MSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00327 207 PLGAAGLAILDELLLMLEHEFIPPTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
102-384 |
2.79e-54 |
|
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: 182.45 E-value: 2.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 102 VPRLGKEAAVKAIKEWG----QPKSKITHLIVCTTSGVD----------------------MPGADYQLTKLLGLRpyVK 155
Cdd:cd00825 11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgadamravgpyvvtkamFPGASGQIATPLGIH--GP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 156 RYMMYQqGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDT------------HLDSLVGQALFGDGAAALI 223
Cdd:cd00825 89 AYDVSA-ACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAmgalstpekasrTFDAAADGFVFGDGAGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 224 VGSDPVP--EIEKPIFEMVWTAQTIAPDSEGAidghlreagltfhllkdvPGIVSKNITKALVEAFEPLGISDYNSIFWI 301
Cdd:cd00825 168 VEELEHAlaRGAHIYAEIVGTAATIDGAGMGA------------------FAPSAEGLARAAKEALAVAGLTVWDIDYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 302 AHPGGPAILDQVEQKL---ALKPEKMNATReVLSEYGNMSSACVLFILDEMRK------KSTQNGL------------KT 360
Cdd:cd00825 230 AHGTGTPIGDVKELKLlrsEFGDKSPAVSA-TKAMTGNLSSAAVVLAVDEAVLmlehgfIPPSIHIeeldeaglnivtET 308
|
330 340
....*....|....*....|....
1CGK_A 361 TGEGLEWGVLFGFGPGLTIETVVL 384
Cdd:cd00825 309 TPRELRTALLNGFGLGGTNATLVL 332
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
16-384 |
7.05e-41 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 146.81 E-value: 7.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 16 PATILAIGTANPANCVEQSTYPDFYFKITNSEHKtelkekfqrmcdksMIKRRYMylteEILKENPNvceymapsldarq 95
Cdd:cd00827 1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTT--------------GIGQRHM----AGDDEDVP------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 96 DMVVvevprlgkEAAVKAIKEWGQPKSKITHLIVCTTSGVD-MPGADYQLTKLLGLRPyVKRYMMyQQGCFAGGTVLRLA 174
Cdd:cd00827 50 TMAV--------EAARRALERAGIDPDDIGLLIVATESPIDkGKSAATYLAELLGLTN-AEAFDL-KQACYGGTAALQLA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 175 KDLAENNKGARVLVVCSEvtavTFRGPSDTHLDslvGQALFGDGAAALIVGSDPVPeiekPIFEMVWTAQTIAP----DS 250
Cdd:cd00827 120 ANLVESGPWRYALVVASD----IASYLLDEGSA---LEPTLGDGAAAMLVSRNPGI----LAAGIVSTHSTSDPgydfSP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 251 EGAIDGHLREAGLTFHLL--------KDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPE 322
Cdd:cd00827 189 YPVMDGGYPKPCKLAYAIrltaepagRAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLGGPPE 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1CGK_A 323 KMNATRE-VLSEYGNMSSACVLFILDEMRKKSTQNGLKTtgeglewGVLFGFGPGLTIETVVL 384
Cdd:cd00827 269 KASQTRWiLLRRVGNMYAASILLGLASLLESGKLKAGDR-------VLLFSYGSGFTAEAFVL 324
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
105-384 |
1.07e-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: 77.20 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 105 LGKEAAVKAIKEWGQPKSKITHLIVCTTSGVD-MPGADYQLTKLLGLrpyvKRYMMY--QQGC--FAGGtvLRLAKDLAE 179
Cdd:cd00830 53 LAVEAAKKALEDAGIDADDIDLIIVATSTPDYlFPATACLVQARLGA----KNAAAFdiNAACsgFLYG--LSTAAGLIR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 180 NNKGARVLVVCSEVTA--VTFRGPSdTHLdslvgqaLFGDGAAALIVG-SDPVPEIEKPIF-------EMVWTAqtiAPD 249
Cdd:cd00830 127 SGGAKNVLVVGAETLSriLDWTDRS-TAV-------LFGDGAGAVVLEaTEEDPGILDSVLgsdgsgaDLLTIP---AGG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 250 SEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGIS----DYnsiFWIaHPGGPAILDQVEQKLALKPEKMN 325
Cdd:cd00830 196 SRSPFEDAEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTpddiDW---FVP-HQANLRIIEAVAKRLGLPEEKVV 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
1CGK_A 326 ATrevLSEYGNMSSACVLFILDEMRKkstQNGLKttgEGlEWGVLFGFGPGLTIETVVL 384
Cdd:cd00830 272 VN---LDRYGNTSAASIPLALDEAIE---EGKLK---KG-DLVLLLGFGAGLTWGAALL 320
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
105-229 |
1.74e-14 |
|
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 442651 [Multi-domain] Cd Length: 382 Bit Score: 74.06 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 105 LGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDM--PGADYqLTKLLGLRPYVkRYMMYQQGCFAGGTVLRLAKDLAENNK 182
Cdd:COG3425 54 MAANAARRALDRAGIDPSDIGAVYVGTESGPDAskPIATY-VHGALGLPPNC-RAFELKFACYAGTAALQAALGWVASGP 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
1CGK_A 183 GARVLVVCSEVtavtfrgpSDTHLDSlVGQALFGDGAAALIVGSDPV 229
Cdd:COG3425 132 NKKALVIASDI--------ARYGPGS-AGEYTQGAGAVAMLVGADPR 169
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
105-385 |
1.24e-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: 70.88 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 105 LGKEAAVKAIKEWGQPKSKITHLIVCTTS-GVDMPGADYQLTKLLGLRPyvKRYMMYQQGCFAGGTVLRLAKDLAENNKG 183
Cdd:TIGR00747 54 MGFEAAKRAIENAGISKDDIDLIIVATTTpDHAFPSAACMVQAYLGIKG--IPAFDLSAACAGFIYALSVAKQYIESGKY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 184 ARVLVVCSEVTAVTF----RGPSdthldslvgqALFGDGAAALIVGSDPVPE--IEKPIF------EMVWTAQTIAPDSE 251
Cdd:TIGR00747 132 KTVLVVGAEKLSSTLdwtdRGTC----------VLFGDGAGAVVLGESEDPGgiISTHLGadgtqgEALYLPAGGRPTSG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 252 GAidGHLREAGltfhllKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMNATrevL 331
Cdd:TIGR00747 202 PS--PFITMEG------NEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKT---V 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
1CGK_A 332 SEYGNMSSACVLFILDEmrkkstqngLKTTGEgLEWG---VLFGFGPGLTIETVVLR 385
Cdd:TIGR00747 271 HKYGNTSAASIPLALDE---------LLRTGR-IKPGdllLLVAFGGGLTWGAALVR 317
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
105-385 |
1.32e-13 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 70.91 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 105 LGKEAAVKAIKEWGQPKSKITHLIVCTTSGvDM--PGADYQLTKLLGLRpyvkrymmyqqGCFA-------GGTV--LRL 173
Cdd:COG0332 54 LAVEAARKALEAAGIDPEDIDLIIVATVTP-DYlfPSTACLVQHKLGAK-----------NAAAfdinaacSGFVyaLSV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 174 AKDLAENNKGARVLVVCSEV-TAVTFRGPSDTHLdslvgqaLFGDGAAALIVGSDpvpEIEKPIFEMVWTAqtiapDSEG 252
Cdd:COG0332 122 AAALIRSGQAKNVLVVGAETlSRIVDWTDRSTCV-------LFGDGAGAVVLEAS---EEGPGILGSVLGS-----DGSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 253 A----IDG-----HLREAGLTFHLL----KDVPGIVSKNITKALVEAFEPLGISdYNSIFWIA-HPGGPAILDQVEQKLA 318
Cdd:COG0332 187 AdllvVPAggsrnPPSPVDEGDHYLrmdgREVFKFAVRNLPEVIREALEKAGLT-LDDIDWFIpHQANLRIIEAVAKRLG 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CGK_A 319 LKPEKMNATrevLSEYGNMSSACVLFILDEMRkkstQNGLKTTGEGLewgVLFGFGPGLTIETVVLR 385
Cdd:COG0332 266 LPEEKVVVN---IDRYGNTSAASIPLALDEAL----REGRIKPGDLV---LLAGFGAGLTWGAAVLR 322
|
|
| PLN02377 |
PLN02377 |
3-ketoacyl-CoA synthase |
150-374 |
1.06e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 166018 Cd Length: 502 Bit Score: 53.48 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 150 LRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-VTAVTFRGPSDThldSLVGQALFGDGAAALIVGSDP 228
Cdd:PLN02377 220 LRGNIRSFNLGGMGCSAGVIAVDLAKDMLQVHRNTYAVVVSTEnITQNWYFGNKKS---MLIPNCLFRVGGSAVLLSNKS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 229 VPEiEKPIFEMVWTAQTiapdSEGAIDGHLR-------EAGLT-FHLLKDVPGI----VSKNIT---------------- 280
Cdd:PLN02377 297 RDK-RRSKYKLVHVVRT----HRGADDKAFRcvyqeqdDAGKTgVSLSKDLMAIageaLKTNITtlgplvlpiseqllff 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 281 ------KALVEAFEPLgISDYNSIF--WIAHPGGPAILDQVEQKLALKPEKMNATREVLSEYGNMSSACVLFILDEMR-K 351
Cdd:PLN02377 372 atlvvkKLFNKKMKPY-IPDFKLAFdhFCIHAGGRAVIDELEKNLQLLPVHVEASRMTLHRFGNTSSSSIWYELAYIEaK 450
|
250 260
....*....|....*....|...
1CGK_A 352 KSTQNGLKTtgegleWGVLFGFG 374
Cdd:PLN02377 451 GRMRKGNRV------WQIAFGSG 467
|
|
| PLN02932 |
PLN02932 |
3-ketoacyl-CoA synthase |
118-374 |
1.99e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 178520 Cd Length: 478 Bit Score: 52.73 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 118 GQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-VTAV 196
Cdd:PLN02932 164 GISPSDIGILVVNSSTFNPTPSLSSILVNKFKLRDNIKSLNLGGMGCSAGVIAIDAAKSLLQVHRNTYALVVSTEnITQN 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 197 TFRGPSDThldSLVGQALFGDGAAALIVgSDPVPEIEKPIFEMVWTAQ--TIAPDS--EGAIDGHLREAGLTFHLLKDVP 272
Cdd:PLN02932 244 LYLGNNKS---MLVTNCLFRIGGAAILL-SNRSRDRKRAKYELVHTVRvhTGADDRsyECATQEEDEDGIVGVSLSKNLP 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 273 GIVSKNItKALVEAFEPL----------------------GISDYNSIFWIA------HPGGPAILDQVEQKLALKPEKM 324
Cdd:PLN02932 320 MVAARTL-KINIATLGPLvlplsekfhffvrfvkkkffnpKLKHYIPDFKLAfehfciHAGGRALIDEMEKNLHLTPLDV 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
1CGK_A 325 NATREVLSEYGNMSSACVLFILDEMRKKstqnGLKTTGEGLeWGVLFGFG 374
Cdd:PLN02932 399 EASRMTLHRFGNTSSSSIWYELAYTEAK----GRMKKGDRI-WQIALGSG 443
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
301-385 |
2.23e-07 |
|
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: 48.27 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 301 IAHPGGPAILDQVEQKLALKPEKMNATrevLSEYGNMSSACVLFILDEMRKkstqNGLKTTGEGLewgVLFGFGPGLTIE 380
Cdd:pfam08541 15 VPHQANLRIIDAVAKRLGLPPEKVVVN---LDEYGNTSAASIPLALDEAVE----EGKLKPGDLV---LLVGFGAGLTWG 84
|
....*
1CGK_A 381 TVVLR 385
Cdd:pfam08541 85 AALLR 89
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
50-374 |
2.95e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 52.28 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 50 TELKEKFQR-MCDKSMIKRRyMYLTEEILKENPNVCeyMAPSLDARQDMVVVEVPRLGKEAAVKaikewgqPKSkITHLI 128
Cdd:PLN02192 134 TEENLEFQRkILERSGLGES-TYLPEAVLNVPPNPC--MAEARKEAETVMFGAIDQLLAKTSVK-------PKD-IGILI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 129 VCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLds 208
Cdd:PLN02192 203 VNCSLFNPTPSLSAMVINHYKLRGNILSYNLGGMGCSAGLISIDLAKHLLQVHPNSYALVISMENITLNWYFGNDRSM-- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 209 LVGQALFGDGAAALIVgSDPVPEIEKPIFEMVWTAQT-------------IAPDSEGAIdghlreaGLTfhLLKDVPGI- 274
Cdd:PLN02192 281 LVSNCLFRMGGAAILL-SNKRSDRRRSKYQLVHTVRThkgaddkcfacvtQEEDSAGKI-------GVS--LSKDLMAVa 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 275 ---VSKNIT----------------------KALVEAFEPLgISDYNSIF--WIAHPGGPAILDQVEQKLALKPEKMNAT 327
Cdd:PLN02192 351 gdaLKTNITtlgplvlpmseqllffatlvgkKLFKMKLKPY-IPDFKLAFehFCIHAGGRAVLDELEKNLQLSDWHMEPS 429
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
1CGK_A 328 REVLSEYGNMSSACVLFILDEMRKKS-TQNGLKTtgegleWGVLFGFG 374
Cdd:PLN02192 430 RMTLYRFGNTSSSSLWYELAYSEAKGrIKKGDRT------WQIAFGSG 471
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
150-374 |
3.20e-07 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 52.27 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 150 LRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLdsLVGQALFGDGAAALIVgSDPV 229
Cdd:PLN02854 236 LRTDIKSYNLGGMGCSAGLISIDLANDLLKANPNSYAVVVSTENITLNWYFGNDRSM--LLCNCIFRMGGAAVLL-SNKA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 230 PEIEKPIFEMVWTAQTiapdSEGAIDGHLR-------EAG-----LTFHLLKDVPGIVSKNIT----------------- 280
Cdd:PLN02854 313 RDRKRSKYQLVHTVRT----HKGADDKNYNcvyqredDKGtigvsLARELMAVAGDALKTNITtlgplvlplseqfmffv 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 281 -----KALVEAFEPLgISDYNSIF--WIAHPGGPAILDQVEQKLALKPEKMNATREVLSEYGNMSSACVLFILDEMRKKs 353
Cdd:PLN02854 389 tlvrrKLLKAKVKPY-IPDFKLAFehFCIHAGGRAVLDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWYELAYTEAK- 466
|
250 260
....*....|....*....|.
1CGK_A 354 tqnGLKTTGEGLeWGVLFGFG 374
Cdd:PLN02854 467 ---GRVSAGDRV-WQIAFGSG 483
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
105-385 |
3.56e-07 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 51.23 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 105 LGKEAAVKAIKEWGQPKSKITHLIVCTTSGVD-MPGADYQLTKLLGLRpyvkrymmyqqGCFA-------GGTV--LRLA 174
Cdd:PRK09352 55 LATEAAKKALEAAGIDPEDIDLIIVATTTPDYaFPSTACLVQARLGAK-----------NAAAfdlsaacSGFVyaLSTA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 175 KDLAENNKGARVLVVCSEV-----------TAVtfrgpsdthldslvgqaLFGDGAAALIVGsdpvpeiekpifemvwta 243
Cdd:PRK09352 124 DQFIRSGAYKNVLVIGAEKlsrivdwtdrsTCV-----------------LFGDGAGAVVLG------------------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 244 qtiAPDSEGAIDGHLREAGLTFHLLKdVPGIVS---------------------KNITKALVEAFEPLGISDyNSIFW-I 301
Cdd:PRK09352 169 ---ASEEPGILSTHLGSDGSYGDLLY-LPGGGSrgpaspgylrmegrevfkfavRELAKVAREALEAAGLTP-EDIDWlV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 302 AHPGGPAILDQVEQKLALKPEKMNATrevLSEYGNMSSACVLFILDEMRkkstQNGLKTTGEGLewgVLFGFGPGLTIET 381
Cdd:PRK09352 244 PHQANLRIIDATAKKLGLPMEKVVVT---VDKYGNTSAASIPLALDEAV----RDGRIKRGDLV---LLEGFGGGLTWGA 313
|
....
1CGK_A 382 VVLR 385
Cdd:PRK09352 314 ALVR 317
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
17-385 |
3.55e-06 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 48.40 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 17 ATILAIGTANPANCVEQSTYPDFyfkITNSEHktelkekfqRMCDKSMIKRRYMylteeilkenpnvceymAPSLDArqd 96
Cdd:CHL00203 3 VHILSTGSSVPNFSVENQQFEDI---IETSDH---------WISTRTGIKKRHL-----------------APSSTS--- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 97 mvvveVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGlrpyVKRYMMYQQGCFAGGTVLRL--A 174
Cdd:CHL00203 51 -----LTKLAAEAANKALDKAHMDPLEIDLIILATSTPDDLFGSASQLQAEIG----ATRAVAFDITAACSGFILALvtA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 175 KDLAENNKGARVLVVcsevtavtfrgPSDTHLDSLVGQ-----ALFGDGAAALIVGSDPVPEIEKpiFEMvwtaqtiapD 249
Cdd:CHL00203 122 TQFIQNGSYKNILVV-----------GADTLSKWIDWSdrktcILFGDGAGAAIIGASYENSILG--FKL---------C 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 250 SEGAIDGHLR---------EAGLT--FHLLKDVPGIVSKNITK--------ALVEAFEPLGISDYNSIFWIAHPGGPAIL 310
Cdd:CHL00203 180 TDGKLNSHLQlmnkpvnnqSFGTTklPQGQYQSISMNGKEVYKfavfqvpaVIIKCLNALNISIDEVDWFILHQANKRIL 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1CGK_A 311 DQVEQKLALKPEKMNATrevLSEYGNMSSACVLFILDE-MRKKSTQNGlkttgeglEWGVLFGFGPGLTIETVVLR 385
Cdd:CHL00203 260 EAIANRLSVPNSKMITN---LEKYGNTSAASIPLALDEaIQNNKIQPG--------QIIVLSGFGAGLTWGAIVLK 324
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
214-385 |
8.25e-05 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 44.34 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 214 LFGDGAAALIVGSDPVPEIEKPIFEM-------------VWTAQTIAPDSEGAIDGHLREAGLTFHLL------------ 268
Cdd:PLN02326 200 LFGDGAGAVVLQACDDDEDGLLGFDMhsdgnghkhlhatFKGEDDDSSGGNTNGVGDFPPKKASYSCIqmngkevfkfav 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 269 KDVPGIVSKNITKALVEAfeplgisdyNSIFW-IAHPGGPAILDQVEQKLALKPEKMNATrevLSEYGNMSSACVLFILD 347
Cdd:PLN02326 280 RCVPQVIESALQKAGLTA---------ESIDWlLLHQANQRIIDAVAQRLGIPPEKVISN---LANYGNTSAASIPLALD 347
|
170 180 190
....*....|....*....|....*....|....*...
1CGK_A 348 EmrkkSTQNGLKTTGEGLEWGvlfGFGPGLTIETVVLR 385
Cdd:PLN02326 348 E----AVRSGKVKKGDVIATA---GFGAGLTWGSAIVR 378
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
105-384 |
8.46e-05 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 44.06 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 105 LGKEAAVKAIKEWGQPKSKITHLI-VCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKG 183
Cdd:PRK07204 55 MGAEAAKKAVEDAKLTLDDIDCIIcASGTIQQAIPCTASLIQEQLGLQHSGIPCFDINSTCLSFITALDTISYAIECGRY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 184 ARVLVVCSEVTAVtfrGPSDTHLDSLVgqaLFGDGAAALIVG-SDPVPEI---------EKPIFEMVWTAQTIAPDSEGA 253
Cdd:PRK07204 135 KRVLIISSEISSV---GLNWGQNESCI---LFGDGAAAVVITkGDHSSRIlashmetysSGAHLSEIRGGGTMIHPREYS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 254 IDghlREAGLTFHLL-KDVPGIVSKNITKALVEAFEPLGISdYNSIFW-IAHPGGPAILDQVEQKLALKPEKMnatREVL 331
Cdd:PRK07204 209 EE---RKEDFLFDMNgRAIFKLSSKYLMKFIDKLLMDAGYT-LADIDLiVPHQASGPAMRLIRKKLGVDEERF---VTIF 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
1CGK_A 332 SEYGNMSSACVLFILDE-MRKKSTQNGLKTtgeglewgVLFGFGPGLTIETVVL 384
Cdd:PRK07204 282 EDHGNMIAASIPVALFEaIKQKKVQRGNKI--------LLLGTSAGLSIGGILL 327
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
161-230 |
1.12e-04 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 40.19 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1CGK_A 161 QQGCfAGGTV-LRLAKDLAENNKGARVLVVCSEV-TAVTFRGPSDTHLdslvgqaLFGDGAAALIVGSDPVP 230
Cdd:pfam08545 4 NAAC-SGFVYaLSTAAALIRSGRAKNVLVIGAETlSKILDWTDRSTAV-------LFGDGAGAVVLEATDEP 67
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
149-280 |
7.92e-04 |
|
FAE1/Type III polyketide synthase-like protein; The members of this family are described as 3-ketoacyl-CoA synthases, type III polyketide synthases, fatty acid elongases and fatty acid condensing enzymes, and are found in both prokaryotic and eukaryotic (mainly plant) species. The region featured in this family contains the active site residues, as well as motifs involved in substrate binding.
Pssm-ID: 429970 Cd Length: 290 Bit Score: 41.08 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CGK_A 149 GLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSE-VTAVTFRGpSDTHLdsLVGQALFGDGAAALIVGSD 227
Cdd:pfam08392 130 KLRSDIKSYNLSGMGCSAGLISIDLAKNLLQVHPNTYALVVSTEnITPNWYFG-NDRSM--LLPNCLFRMGGAAVLLSNR 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
1CGK_A 228 PVpEIEKPIFEMVWTAQTiapdSEGAIDGHLR-------EAGLT-FHLLKDVPGIVS----KNIT 280
Cdd:pfam08392 207 PA-DRRRAKYELVHTVRT----HKGADDRAYNcvyqeedEDGKVgVSLSKDLMKVAGralkTNIT 266
|
|
| |
