BLASTX 2.2.25 [Feb-01-2011]


Reference: Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schaffer, 
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997), 
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs",  Nucleic Acids Res. 25:3389-3402.

Query= Coptis21_contig00018217
         (606 letters)

Database: ./nr 
           23,641,837 sequences; 8,123,359,852 total letters

Searching..................................................done



                                                                 Score    E
Sequences producing significant alignments:                      (bits) Value

gb|ABA86595.1| putative dihydroflavonol 4-reductase [Aquilegia f...   229   4e-58
gb|AFG28176.1| putative dihydroflavonol 4-reductase [Vitis bellula]   219   4e-55
pdb|2C29|D Chain D, Structure Of Dihydroflavonol Reductase From ...   216   2e-54
sp|P51110.1|DFRA_VITVI RecName: Full=Dihydroflavonol-4-reductase...   216   2e-54
emb|CBI19727.3| unnamed protein product [Vitis vinifera]              216   2e-54

>gb|ABA86595.1| putative dihydroflavonol 4-reductase [Aquilegia formosa]
          Length = 269

 Score =  229 bits (583), Expect = 4e-58
 Identities = 106/123 (86%), Positives = 117/123 (95%)
 Frame = +3

Query: 90  DNIKKVKHLLDMPNAKTNLTLWKADLVNEGSFDDAIKGCSGVFHVATPMDFESRDPENEV 269
           DN+KKV+HLLD+P AKTNLTLWKADLV+EGSFDDAI+ C+GVFHVATPMDFES+DPENEV
Sbjct: 1   DNLKKVQHLLDLPYAKTNLTLWKADLVDEGSFDDAIEECTGVFHVATPMDFESKDPENEV 60

Query: 270 IKPTIEGMLNIMRSCVKAKIVRRLVFTSSAGTVNVQEHQQPAYD*NCWTDIEFCRTKKMT 449
           IKPTIEGMLNIMRSC+KAK VRRLVFTSSAGTVNV+EHQQP YD NCWTDI+ CRTKKMT
Sbjct: 61  IKPTIEGMLNIMRSCLKAKTVRRLVFTSSAGTVNVEEHQQPEYDENCWTDIDICRTKKMT 120

Query: 450 GWV 458
           GW+
Sbjct: 121 GWM 123


>gb|AFG28176.1| putative dihydroflavonol 4-reductase [Vitis bellula]
          Length = 337

 Score =  219 bits (557), Expect = 4e-55
 Identities = 105/152 (69%), Positives = 122/152 (80%)
 Frame = +3

Query: 93  NIKKVKHLLDMPNAKTNLTLWKADLVNEGSFDDAIKGCSGVFHVATPMDFESRDPENEVI 272
           N+KKVKHLLD+P A+T+LTLWKADL +EGSFD+AIKGC+GVFHVATPMDFES+DPENEVI
Sbjct: 41  NVKKVKHLLDLPKAETHLTLWKADLADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVI 100

Query: 273 KPTIEGMLNIMRSCVKAKIVRRLVFTSSAGTVNVQEHQQPAYD*NCWTDIEFCRTKKMTG 452
           KPTIEGML IM+SC  AK VRRLVFTSSAGTVN+QEHQ P YD +CW+D+EFCR KKMTG
Sbjct: 101 KPTIEGMLGIMKSCAAAKTVRRLVFTSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTG 160

Query: 453 WVCHFAFFNFESYAMNHAKIMEIGVFRMIVRL 548
           W+   +    E  A  +AK   I    +I  L
Sbjct: 161 WMYFVSKTLAEQAAWKYAKENNIDFISIIPTL 192


>pdb|2C29|D Chain D, Structure Of Dihydroflavonol Reductase From Vitis Vinifera
           At 1.8 A. gi|118137402|pdb|2C29|F Chain F, Structure Of
           Dihydroflavonol Reductase From Vitis Vinifera At 1.8 A.
           gi|158428822|pdb|2IOD|A Chain A, Binding Of Two
           Substrate Analogue Molecules To
           Dihydroflavonol-4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|158428823|pdb|2IOD|B
           Chain B, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol-4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|158428824|pdb|2IOD|C
           Chain C, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol-4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|158428825|pdb|2IOD|D
           Chain D, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol-4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|160285642|pdb|2NNL|D
           Chain D, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol-4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|160285643|pdb|2NNL|F
           Chain F, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol-4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|168177310|pdb|3C1T|A
           Chain A, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|168177311|pdb|3C1T|B
           Chain B, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|168177312|pdb|3C1T|C
           Chain C, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|168177313|pdb|3C1T|D
           Chain D, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|209870409|pdb|3BXX|A
           Chain A, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|209870410|pdb|3BXX|B
           Chain B, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|209870411|pdb|3BXX|C
           Chain C, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|209870412|pdb|3BXX|D
           Chain D, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|209870413|pdb|3BXX|E
           Chain E, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site gi|209870414|pdb|3BXX|F
           Chain F, Binding Of Two Substrate Analogue Molecules To
           Dihydroflavonol 4-Reductase Alters The Functional
           Geometry Of The Catalytic Site
           gi|1888485|emb|CAA72420.1| dihydroflavonol 4-reductase
           [Vitis vinifera] gi|59939328|gb|AAX12423.1|
           dihydroflavonol 4-reductase [Vitis vinifera]
          Length = 337

 Score =  216 bits (551), Expect = 2e-54
 Identities = 104/152 (68%), Positives = 121/152 (79%)
 Frame = +3

Query: 93  NIKKVKHLLDMPNAKTNLTLWKADLVNEGSFDDAIKGCSGVFHVATPMDFESRDPENEVI 272
           N+KKVKHLLD+P A+T+LTLWKADL +EGSFD+AIKGC+GVFHVATPMDFES+DPENEVI
Sbjct: 41  NVKKVKHLLDLPKAETHLTLWKADLADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVI 100

Query: 273 KPTIEGMLNIMRSCVKAKIVRRLVFTSSAGTVNVQEHQQPAYD*NCWTDIEFCRTKKMTG 452
           KPTIEGML IM+SC  AK VRRLVFTSSAGTVN+QEHQ P YD +CW+D+EFCR KKMT 
Sbjct: 101 KPTIEGMLGIMKSCAAAKTVRRLVFTSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTA 160

Query: 453 WVCHFAFFNFESYAMNHAKIMEIGVFRMIVRL 548
           W+   +    E  A  +AK   I    +I  L
Sbjct: 161 WMYFVSKTLAEQAAWKYAKENNIDFITIIPTL 192


>sp|P51110.1|DFRA_VITVI RecName: Full=Dihydroflavonol-4-reductase; Short=DFR; AltName:
           Full=Dihydrokaempferol 4-reductase
           gi|499018|emb|CAA53578.1| dihydroflavonol reductase
           [Vitis vinifera]
          Length = 337

 Score =  216 bits (551), Expect = 2e-54
 Identities = 104/152 (68%), Positives = 121/152 (79%)
 Frame = +3

Query: 93  NIKKVKHLLDMPNAKTNLTLWKADLVNEGSFDDAIKGCSGVFHVATPMDFESRDPENEVI 272
           N+KKVKHLLD+P A+T+LTLWKADL +EGSFD+AIKGC+GVFHVATPMDFES+DPENEVI
Sbjct: 41  NVKKVKHLLDLPKAETHLTLWKADLADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVI 100

Query: 273 KPTIEGMLNIMRSCVKAKIVRRLVFTSSAGTVNVQEHQQPAYD*NCWTDIEFCRTKKMTG 452
           KPTIEGML IM+SC  AK VRRLVFTSSAGTVN+QEHQ P YD +CW+D+EFCR KKMT 
Sbjct: 101 KPTIEGMLGIMKSCAAAKTVRRLVFTSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTA 160

Query: 453 WVCHFAFFNFESYAMNHAKIMEIGVFRMIVRL 548
           W+   +    E  A  +AK   I    +I  L
Sbjct: 161 WMYFVSKTLAEQAAWKYAKENNIDFITIIPTL 192


>emb|CBI19727.3| unnamed protein product [Vitis vinifera]
          Length = 931

 Score =  216 bits (551), Expect = 2e-54
 Identities = 104/152 (68%), Positives = 121/152 (79%)
 Frame = +3

Query: 93   NIKKVKHLLDMPNAKTNLTLWKADLVNEGSFDDAIKGCSGVFHVATPMDFESRDPENEVI 272
            N+KKVKHLLD+P A+T+LTLWKADL +EGSFD+AIKGC+GVFHVATPMDFES+DPENEVI
Sbjct: 635  NVKKVKHLLDLPKAETHLTLWKADLADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVI 694

Query: 273  KPTIEGMLNIMRSCVKAKIVRRLVFTSSAGTVNVQEHQQPAYD*NCWTDIEFCRTKKMTG 452
            KPTIEGML IM+SC  AK VRRLVFTSSAGTVN+QEHQ P YD +CW+D+EFCR KKMT 
Sbjct: 695  KPTIEGMLGIMKSCAAAKTVRRLVFTSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTA 754

Query: 453  WVCHFAFFNFESYAMNHAKIMEIGVFRMIVRL 548
            W+   +    E  A  +AK   I    +I  L
Sbjct: 755  WMYFVSKTLAEQAAWKYAKENNIDFITIIPTL 786



 Score =  162 bits (410), Expect = 4e-38
 Identities = 74/140 (52%), Positives = 102/140 (72%), Gaps = 1/140 (0%)
 Frame = +3

Query: 93  NIKKVKHLLDMPNAKTNLTLWKADLVNEGSFDDAIKGCSGVFHVATPMDFESRDPENEVI 272
           N++KVKHLL++P A T+L+LW+ADL  EGSFDDAI+GC GVFHVA+PMD  ++D +NEVI
Sbjct: 42  NVEKVKHLLELPKASTHLSLWRADLKEEGSFDDAIQGCIGVFHVASPMDISTQDAQNEVI 101

Query: 273 KPTIEGMLNIMRSCVKAKIVRRLVFTSSAGTVNVQEHQQP-AYD*NCWTDIEFCRTKKMT 449
            PT+ G+L+IMR+C KAK V+R ++TS+ GT+ V     P  YD + WTD+++C+ +KMT
Sbjct: 102 DPTVNGVLDIMRACTKAKTVKRFIYTSTTGTITVGPEPLPLEYDESFWTDVDYCKAQKMT 161

Query: 450 GWVCHFAFFNFESYAMNHAK 509
            W+   A    E  A   AK
Sbjct: 162 AWMYFIAKTTAEKAAWEFAK 181