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Conserved domains on  [gi|442772337|gb|AGC72962|]
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chalcone synthase, partial [Pseudodraba hystrix]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03172 super family cl30448
chalcone synthase family protein; Provisional
 1-306 0e+00

chalcone synthase family protein; Provisional


The actual alignment was detected with superfamily member PLN03172:

Pssm-ID: 178716  Cd Length: 393  Bit Score: 568.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:PLN03172  16 PATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKENPNMCAYMAPSLDARQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:PLN03172  96 DMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMYQQGCFAGGTVLRLAK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDASVgEKPIFEMVSAAQTILPDSDGAI 240
Cdd:PLN03172 176 DLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKI-ERPLFEIVSAAQTILPDSDGAI 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442772337 241 DGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:PLN03172 255 DGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
 
Name Accession Description Interval E-value
PLN03172 PLN03172
chalcone synthase family protein; Provisional
 1-306 0e+00

chalcone synthase family protein; Provisional


Pssm-ID: 178716  Cd Length: 393  Bit Score: 568.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:PLN03172  16 PATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKENPNMCAYMAPSLDARQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:PLN03172  96 DMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMYQQGCFAGGTVLRLAK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDASVgEKPIFEMVSAAQTILPDSDGAI 240
Cdd:PLN03172 176 DLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKI-ERPLFEIVSAAQTILPDSDGAI 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442772337 241 DGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:PLN03172 255 DGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
Chal_sti_synt_N pfam00195
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ...
 1-213 8.05e-142

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: 398.84  E-value: 8.05e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337    1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:pfam00195  13 KATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPELCTEMAPSLDARL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:pfam00195  93 EIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQGCYGGATVLRTAK 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442772337  161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDP 213
Cdd:pfam00195 173 DIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 1-306 1.27e-136

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: 390.82  E-value: 1.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLT--EEFLKDNPKMcaymAPSLDA 78
Cdd:cd00831    1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPEM----SPSLDE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  79 RQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRL 158
Cdd:cd00831   77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 159 AKDLAENNRGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFSDGAAALIVGSDPDASVGEKPIFEMVSAAQTILPDSDG 238
Cdd:cd00831  157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRRERPLFELVRAASTLLPDSED 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 239 AIDGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPL--GISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:cd00831  235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLS 304
BH0617 COG3424
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ...
 4-305 3.47e-67

Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442650 [Multi-domain]  Cd Length: 351  Bit Score: 213.46  E-value: 3.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   4 ILAIGTANPANHVIQAEYPDYyFRITNSEHMTDLkEKFKRMCDKSMIRKRHMHLTEEFLKDNPkmcaymapSLDARQDIV 83
Cdd:COG3424    4 ILSIATAVPPHRYTQEEIAEF-AAELFGLDERDR-RRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERNALY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  84 VVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLA 163
Cdd:COG3424   74 IEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 164 ENNRGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFSDGAAALIVGSDPDASVGekpiFEMVSAAQTILPDSDGAIDGH 243
Cdd:COG3424  154 RADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPGPG----PRILAFRSYLIPDTEDVMGWD 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442772337 244 LREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGL 305
Cdd:COG3424  229 VGDTGFRMVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGL 290
 
Name Accession Description Interval E-value
PLN03172 PLN03172
chalcone synthase family protein; Provisional
 1-306 0e+00

chalcone synthase family protein; Provisional


Pssm-ID: 178716  Cd Length: 393  Bit Score: 568.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:PLN03172  16 PATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKENPNMCAYMAPSLDARQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:PLN03172  96 DMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMYQQGCFAGGTVLRLAK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDASVgEKPIFEMVSAAQTILPDSDGAI 240
Cdd:PLN03172 176 DLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKI-ERPLFEIVSAAQTILPDSDGAI 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442772337 241 DGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:PLN03172 255 DGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
PLN03173 PLN03173
chalcone synthase; Provisional
 1-306 0e+00

chalcone synthase; Provisional


Pssm-ID: 178717 [Multi-domain]  Cd Length: 391  Bit Score: 561.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:PLN03173  16 PATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKENPSVCEYMAPSLDARQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:PLN03173  96 DMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMYQQGCFAGGTVLRLAK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDASVgEKPIFEMVSAAQTILPDSDGAI 240
Cdd:PLN03173 176 DLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGV-EKPLFELVSAAQTILPDSDGAI 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442772337 241 DGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:PLN03173 255 DGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALK 320
PLN03170 PLN03170
chalcone synthase; Provisional
 1-306 0e+00

chalcone synthase; Provisional


Pssm-ID: 178714 [Multi-domain]  Cd Length: 401  Bit Score: 559.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:PLN03170  20 PATVLAIGTATPANCVHQADYPDYYFRITKSEHMTELKEKFKRMCDKSQIRKRYMHLTEEYLAENPNMCAYMAPSLDARQ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:PLN03170 100 DIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNRLMMYQQGCFAGGTVLRVAK 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDASVgEKPIFEMVSAAQTILPDSDGAI 240
Cdd:PLN03170 180 DLAENNRGARVLVVCSEITAVTFRGPSESHLDSMVGQALFGDGAAAVIVGADPDERV-ERPLFQLVSASQTILPDSEGAI 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442772337 241 DGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:PLN03170 259 DGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAKVGLE 324
PLN03168 PLN03168
chalcone synthase; Provisional
 1-305 3.45e-164

chalcone synthase; Provisional


Pssm-ID: 178712 [Multi-domain]  Cd Length: 389  Bit Score: 461.82  E-value: 3.45e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:PLN03168  15 PACVLGIGTAVPPAEFLQSEYPDFFFNITNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVLKANPGICTYMEPSLNVRH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:PLN03168  95 DIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGADHALAKLLGLKPTVKRVMMYQTGCFGGASVLRVAK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDASVgEKPIFEMVSAAQTILPDSDGAI 240
Cdd:PLN03168 175 DLAENNKGARVLAVASEVTAVTYRAPSENHLDGLVGSALFGDGAGVYVVGSDPKPEV-EKALFEVHWAGETILPESDGAI 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442772337 241 DGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGL 305
Cdd:PLN03168 254 DGHLTEAGLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKL 318
Chal_sti_synt_N pfam00195
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ...
 1-213 8.05e-142

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: 398.84  E-value: 8.05e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337    1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:pfam00195  13 KATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPELCTEMAPSLDARL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:pfam00195  93 EIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQGCYGGATVLRTAK 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442772337  161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDP 213
Cdd:pfam00195 173 DIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 1-306 1.27e-136

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: 390.82  E-value: 1.27e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLT--EEFLKDNPKMcaymAPSLDA 78
Cdd:cd00831    1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPEM----SPSLDE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  79 RQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRL 158
Cdd:cd00831   77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 159 AKDLAENNRGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFSDGAAALIVGSDPDASVGEKPIFEMVSAAQTILPDSDG 238
Cdd:cd00831  157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRRERPLFELVRAASTLLPDSED 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 239 AIDGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPL--GISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:cd00831  235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLS 304
PLN03171 PLN03171
chalcone synthase-like protein; Provisional
 1-306 7.37e-136

chalcone synthase-like protein; Provisional


Pssm-ID: 178715 [Multi-domain]  Cd Length: 399  Bit Score: 390.52  E-value: 7.37e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQ 80
Cdd:PLN03171  22 LAAVLAIGTANPANCVPQDEFPDFYFRATKSDHLTALKDKFKRICQELGVQKRYLHHTEELLSAHPEFLDHDAPSLDARL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 DIVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAK 160
Cdd:PLN03171 102 DIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAHIPGVDFRLVPLLGLRPSVRRTMLHLNGCFAGAAALRLAK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 161 DLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDASvgEKPIFEMVSAAQTILPDSDGAI 240
Cdd:PLN03171 182 DLAENNRGARVLVVAAEITLLLFNGPDEGCFQTLLNQGLFGDGAAAVIVGADADAA--ERPLFEIVSAAQAIIPESDDAI 259

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442772337 241 DGHLREVGLTFHL-LKDVPGLVSKNIEKSLDEAFKPL----GISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:PLN03171 260 NMHFTEGGLDGNIgTRQVPGLIGDNIERCLLDAFAPLlggdGGAEWNDLFWAVHPGSSAILDQVDAALGLE 330
PLN03169 PLN03169
chalcone synthase family protein; Provisional
 2-306 4.94e-97

chalcone synthase family protein; Provisional


Pssm-ID: 215612 [Multi-domain]  Cd Length: 391  Bit Score: 291.22  E-value: 4.94e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   2 AGILAIGTANPANHVIQAEYPDYYFRITNSEHmTDLKEKFKRMCDKSMIRKRHMHLTEEFLKDNPKMCAYMAPSLDARQD 81
Cdd:PLN03169  22 ATILALGKAFPSQLVPQEYLVDGYFRDTKCDD-PALKEKLERLCKTTTVKTRYVVMSKEILDKYPELATEGTPTIKQRLD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  82 IVVVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKD 161
Cdd:PLN03169 101 IANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEARLPGGDLYLAKQLGLSPDVQRVMLYFLGCSGGVAGLRVAKD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 162 LAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDAsVGEKPIFEMVSAAQTILPDSDGAID 241
Cdd:PLN03169 181 IAENNPGSRVLLTTSETTILGFRPPSPDRPYDLVGAALFGDGAAAVIIGADPIP-VSESPFFELHTAIQQFLPGTEKTID 259

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442772337 242 GHLREVGLTFHLLKDVPGLVSKNIE----KSLDEAfkPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:PLN03169 260 GRLTEEGINFKLGRELPQKIEDNIEgfckKLMKKA--GLVEKDYNDLFWAVHPGGPAILNRLEKKLKLA 326
BH0617 COG3424
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ...
 4-305 3.47e-67

Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442650 [Multi-domain]  Cd Length: 351  Bit Score: 213.46  E-value: 3.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   4 ILAIGTANPANHVIQAEYPDYyFRITNSEHMTDLkEKFKRMCDKSMIRKRHMHLTEEFLKDNPkmcaymapSLDARQDIV 83
Cdd:COG3424    4 ILSIATAVPPHRYTQEEIAEF-AAELFGLDERDR-RRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERNALY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  84 VVEVPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLA 163
Cdd:COG3424   74 IEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 164 ENNRGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFSDGAAALIVGSDPDASVGekpiFEMVSAAQTILPDSDGAIDGH 243
Cdd:COG3424  154 RADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPGPG----PRILAFRSYLIPDTEDVMGWD 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442772337 244 LREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGL 305
Cdd:COG3424  229 VGDTGFRMVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGL 290
Chal_sti_synt_C pfam02797
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ...
 224-306 6.14e-45

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: 149.91  E-value: 6.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  224 EMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKL 303
Cdd:pfam02797   1 ELVSAAQTFLPNTDGVIDGHLTEEGLTFHLGRDVPQKIEENIEEFLKKAFEPLGISEWNSLFWIVHPGGPAILDRVETKL 80


                  ...
gi 442772337  304 GLK 306
Cdd:pfam02797  81 GLE 83
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 87-307 1.17e-41

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: 147.01  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  87 VPKLGKEAAVKAIKEWG----QPKSKITHPVFCTTSGVD----------------------MPGADYQLTKLLGLrpSVK 140
Cdd:cd00825   11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgadamravgpyvvtkamFPGASGQIATPLGI--HGP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 141 RLMMYQqGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDT------------HLDSLVGQALFSDGAAALI 208
Cdd:cd00825   89 AYDVSA-ACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAmgalstpekasrTFDAAADGFVFGDGAGALV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 209 VGSDPDASV-GEKPIFEMVSAAQTILPDSDGAidghlrevgltfhllkdvPGLVSKNIEKSLDEAFKPLGISDWNSLFWI 287
Cdd:cd00825  168 VEELEHALArGAHIYAEIVGTAATIDGAGMGA------------------FAPSAEGLARAAKEALAVAGLTVWDIDYLV 229

                        250       260
                 ....*....|....*....|
gi 442772337 288 AHPGGPAILDQVEIKLGLKA 307
Cdd:cd00825  230 AHGTGTPIGDVKELKLLRSE 249
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 87-307 9.27e-41

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: 142.20  E-value: 9.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  87 VPKLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVD-MPGADYQLTKLLGLrPSVKRLMMYQqGCFAGGTVLRLAKDLAEN 165
Cdd:cd00327    7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGeFSGAAGQLAYHLGI-SGGPAYSVNQ-ACATGLTALALAVQQVQN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 166 NRGARVLVVCSEItavtfrgpsdthldslvgqALFSDGAAALIVGSDPDASV-GEKPIFEMVSAAQTILPDSDgaidghl 244
Cdd:cd00327   85 GKADIVLAGGSEE-------------------FVFGDGAAAAVVESEEHALRrGAHPQAEIVSTAATFDGASM------- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442772337 245 revgltfhllkdVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKA 307
Cdd:cd00327  139 ------------VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDP 189
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 1-306 5.90e-26

"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: 104.82  E-value: 5.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   1 PAGILAIGTANPANHVIQAEYPDYYFRITNSEHMtdlkekfkrmcdksMIRKRHMHLTEEflkDNPKMCAymapsldarq 80
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTT--------------GIGQRHMAGDDE---DVPTMAV---------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  81 divvvevpklgkEAAVKAIKEWGQPKSKITHPVFCTTSGVD-MPGADYQLTKLLGLRPSvkRLMMYQQGCFAGGTVLRLA 159
Cdd:cd00827   54 ------------EAARRALERAGIDPDDIGLLIVATESPIDkGKSAATYLAELLGLTNA--EAFDLKQACYGGTAALQLA 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 160 KDLAENNRGARVLVVCSEItavtFRGPSDTHLDslvGQALFSDGAAALIVGSDPDASvgekpIFEMVSAAQTILPDSD-- 237
Cdd:cd00827  120 ANLVESGPWRYALVVASDI----ASYLLDEGSA---LEPTLGDGAAAMLVSRNPGIL-----AAGIVSTHSTSDPGYDfs 187

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442772337 238 --GAIDGHLREVGLTFHLL--------KDVPGLVSKNIEKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 306
Cdd:cd00827  188 pyPVMDGGYPKPCKLAYAIrltaepagRAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLGGP 266
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 80-214 6.06e-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: 71.36  E-value: 6.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  80 QDIVVvevpkLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVDM--PGADYqLTKLLGLRPSVkRLMMYQQGCFAGGTVLR 157
Cdd:COG3425   49 EDAVT-----MAANAARRALDRAGIDPSDIGAVYVGTESGPDAskPIATY-VHGALGLPPNC-RAFELKFACYAGTAALQ 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442772337 158 LAKDLAENNRGARVLVVCSEItavtfrgpSDTHLDSlVGQALFSDGAAALIVGSDPD 214
Cdd:COG3425  122 AALGWVASGPNKKALVIASDI--------ARYGPGS-AGEYTQGAGAVAMLVGADPR 169
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
 146-218 3.17e-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: 38.65  E-value: 3.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442772337  146 QQGCfAGGTV-LRLAKDLAENNRGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFSDGAAALIVGSDPDASVG 218
Cdd:pfam08545   4 NAAC-SGFVYaLSTAAALIRSGRAKNVLVIGAETlSKILDWTDRSTAV-------LFGDGAGAVVLEATDEPGAR 70
FAE1_CUT1_RppA pfam08392
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ...
 134-226 3.37e-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: 41.46  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  134 GLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSE-ITAVTFRGpSDTHLdsLVGQALFSDGAAALIVGSD 212
Cdd:pfam08392 130 KLRSDIKSYNLSGMGCSAGLISIDLAKNLLQVHPNTYALVVSTEnITPNWYFG-NDRSM--LLPNCLFRMGGAAVLLSNR 206

                          90
                  ....*....|....
gi 442772337  213 PDASVGEKpiFEMV 226
Cdd:pfam08392 207 PADRRRAK--YELV 218
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
90-281 1.05e-03

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 40.20  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  90 LGKEAAVKAIKEWGQPKSKITHPV-FCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRG 168
Cdd:PRK07204  55 MGAEAAKKAVEDAKLTLDDIDCIIcASGTIQQAIPCTASLIQEQLGLQHSGIPCFDINSTCLSFITALDTISYAIECGRY 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 169 ARVLVVCSEITAVtfrGPSDTHLDSLVgqaLFSDGAAALIVGSDPDAS---------VGEKPIFEMVSAAQTILPDSDGA 239
Cdd:PRK07204 135 KRVLIISSEISSV---GLNWGQNESCI---LFGDGAAAVVITKGDHSSrilashmetYSSGAHLSEIRGGGTMIHPREYS 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 442772337 240 IDghlREVGLTFHLL-KDVPGLVSKNIEKSLDEAFKPLGIS----DW 281
Cdd:PRK07204 209 EE---RKEDFLFDMNgRAIFKLSSKYLMKFIDKLLMDAGYTladiDL 252
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 2-305 4.90e-03

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: 37.90  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337   2 AGILAIGTANPANhviqaeypdyyfRITNSE--HMTDLKEKFKRmcDKSMIRKRHMHLTEEFLKDnpkmcaymapsldar 79
Cdd:cd00830    2 ARILGIGSYLPER------------VVTNDEleKRLDTSDEWIR--TRTGIRERRIADPGETTSD--------------- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337  80 qdivvvevpkLGKEAAVKAIKEWGQPKSKITHPVFCTTSGVD-MPGADYQLTKLLGLrpsvKRLMMY--QQGC--FAGGt 154
Cdd:cd00830   53 ----------LAVEAAKKALEDAGIDADDIDLIIVATSTPDYlFPATACLVQARLGA----KNAAAFdiNAACsgFLYG- 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 155 vLRLAKDLAENNRGARVLVVCSEITA--VTFRGPSdTHLdslvgqaLFSDGAAALIVGSDPDA---------SVGEKPIF 223
Cdd:cd00830  118 -LSTAAGLIRSGGAKNVLVVGAETLSriLDWTDRS-TAV-------LFGDGAGAVVLEATEEDpgildsvlgSDGSGADL 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442772337 224 EMVSAAQTILPDSDGAIDGHL-----REVgltfhlLKDVPGLVSKNIEKSLDEA-FKPLGIsDWnslFWIaHPGGPAILD 297
Cdd:cd00830  189 LTIPAGGSRSPFEDAEGGDPYlvmdgREV------FKFAVRLMPESIEEALEKAgLTPDDI-DW---FVP-HQANLRIIE 257


                 ....*...
gi 442772337 298 QVEIKLGL 305
Cdd:cd00830  258 AVAKRLGL 265
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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