BLASTX nr result
ID: Aconitum21_contig00012637
seq
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= Aconitum21_contig00012637
(1164 letters)
Database: ./nr
23,641,837 sequences; 8,123,359,852 total letters
Searching..................................................done
Score E
Sequences producing significant alignments: (bits) Value
dbj|BAF49325.1| dihydroflavonol 4-reductase [Delphinium x bellad... 597 e-168
gb|AFG28176.1| putative dihydroflavonol 4-reductase [Vitis bellula] 527 e-147
pdb|2C29|D Chain D, Structure Of Dihydroflavonol Reductase From ... 526 e-147
emb|CBI19727.3| unnamed protein product [Vitis vinifera] 526 e-147
ref|XP_002281858.1| PREDICTED: dihydroflavonol-4-reductase [Viti... 526 e-147
>dbj|BAF49325.1| dihydroflavonol 4-reductase [Delphinium x belladonna]
Length = 337
Score = 597 bits (1540), Expect = e-168
Identities = 285/328 (86%), Positives = 309/328 (94%)
Frame = +3
Query: 114 MTVETLCVTGAAGFIGSWLVMRLLERGYVVRATVRDPDNLKKVSHLLELPNAKNKLTLWK 293
MTVET+CVTGAAGFIGSWLVMRLLERGY+VRATVR+PDNLKK+ HLLELPNAK+KLTLWK
Sbjct: 1 MTVETVCVTGAAGFIGSWLVMRLLERGYLVRATVRNPDNLKKLRHLLELPNAKSKLTLWK 60
Query: 294 ADLADEGSYDDVIKGCTGVFHVATPMDFESKDPENEVIKPTIEGLLSIMKSCVKAKSVRR 473
ADL ++GSYDD IKGCTGVFHVATPMDFESKDPENEVIKPTIEG+L IMKSCVKAKSVRR
Sbjct: 61 ADLTEDGSYDDAIKGCTGVFHVATPMDFESKDPENEVIKPTIEGMLGIMKSCVKAKSVRR 120
Query: 474 LVFTSSAGTVNVQEHQQDEYDESSWTDIEFCRTKKMTGWMYFVSKTLAEKAAWEFTERNN 653
LVFTSSAG+VNV+E QQ EYDE+SWTD+EFCRT+KMTGWMYFVSKTLAEKAAWEF ++NN
Sbjct: 121 LVFTSSAGSVNVEERQQAEYDENSWTDVEFCRTRKMTGWMYFVSKTLAEKAAWEFAQQNN 180
Query: 654 IDFISIIPTLVVGPFLVPSMPPSLITALSPITGNEPHYSILKQIQLVHLDDLCNAHIYLF 833
IDFISIIPTLVVGPFL+PSMPPSLITALSPITGN+ HYSILKQIQLVHLDDLCNAHIYLF
Sbjct: 181 IDFISIIPTLVVGPFLMPSMPPSLITALSPITGNQSHYSILKQIQLVHLDDLCNAHIYLF 240
Query: 834 EHPEANGRYICSSHNATITDVANLLKQKFPEYSVPTKFEGIDEKLKVVAFSSKRLKDLGF 1013
EHPE+NGRYICSSH+ATITDVANLL+ KFPEY+VPTKF G+DE LK V FSSKRLKDLGF
Sbjct: 241 EHPESNGRYICSSHDATITDVANLLRHKFPEYNVPTKFMGVDENLKAVVFSSKRLKDLGF 300
Query: 1014 NYKYNMADMFVSAVATCRRKGILPLSNQ 1097
NYKY M DMFV AV TCRR GILP +N+
Sbjct: 301 NYKYTMEDMFVGAVTTCRRNGILPFTNK 328
>gb|AFG28176.1| putative dihydroflavonol 4-reductase [Vitis bellula]
Length = 337
Score = 527 bits (1358), Expect = e-147
Identities = 247/325 (76%), Positives = 288/325 (88%)
Frame = +3
Query: 123 ETLCVTGAAGFIGSWLVMRLLERGYVVRATVRDPDNLKKVSHLLELPNAKNKLTLWKADL 302
ET+CVTGA+GFIGSWLVMRLLERGY VRATVRDP N+KKV HLL+LP A+ LTLWKADL
Sbjct: 6 ETVCVTGASGFIGSWLVMRLLERGYTVRATVRDPTNVKKVKHLLDLPKAETHLTLWKADL 65
Query: 303 ADEGSYDDVIKGCTGVFHVATPMDFESKDPENEVIKPTIEGLLSIMKSCVKAKSVRRLVF 482
ADEGS+D+ IKGCTGVFHVATPMDFESKDPENEVIKPTIEG+L IMKSC AK+VRRLVF
Sbjct: 66 ADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVIKPTIEGMLGIMKSCAAAKTVRRLVF 125
Query: 483 TSSAGTVNVQEHQQDEYDESSWTDIEFCRTKKMTGWMYFVSKTLAEKAAWEFTERNNIDF 662
TSSAGTVN+QEHQ YDES W+D+EFCR KKMTGWMYFVSKTLAE+AAW++ + NNIDF
Sbjct: 126 TSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTGWMYFVSKTLAEQAAWKYAKENNIDF 185
Query: 663 ISIIPTLVVGPFLVPSMPPSLITALSPITGNEPHYSILKQIQLVHLDDLCNAHIYLFEHP 842
ISIIPTLVVGPF++ SMPPSLITALSPITGNE HYSI++Q Q VHLDDLCNAHIYLFE+P
Sbjct: 186 ISIIPTLVVGPFIMSSMPPSLITALSPITGNEAHYSIIRQGQFVHLDDLCNAHIYLFENP 245
Query: 843 EANGRYICSSHNATITDVANLLKQKFPEYSVPTKFEGIDEKLKVVAFSSKRLKDLGFNYK 1022
+A GRYICSS++ I D+A +L++K+PEY++PT+F+G+DE LK V FSSK+L DLGF +K
Sbjct: 246 KAEGRYICSSNDCIILDLAKMLREKYPEYNIPTEFKGVDENLKSVCFSSKKLTDLGFEFK 305
Query: 1023 YNMADMFVSAVATCRRKGILPLSNQ 1097
Y++ DMF AV TCR KG+LP S++
Sbjct: 306 YSLEDMFTGAVDTCRAKGLLPPSHE 330
>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 = 526 bits (1356), Expect = e-147
Identities = 246/325 (75%), Positives = 287/325 (88%)
Frame = +3
Query: 123 ETLCVTGAAGFIGSWLVMRLLERGYVVRATVRDPDNLKKVSHLLELPNAKNKLTLWKADL 302
ET+CVTGA+GFIGSWLVMRLLERGY VRATVRDP N+KKV HLL+LP A+ LTLWKADL
Sbjct: 6 ETVCVTGASGFIGSWLVMRLLERGYTVRATVRDPTNVKKVKHLLDLPKAETHLTLWKADL 65
Query: 303 ADEGSYDDVIKGCTGVFHVATPMDFESKDPENEVIKPTIEGLLSIMKSCVKAKSVRRLVF 482
ADEGS+D+ IKGCTGVFHVATPMDFESKDPENEVIKPTIEG+L IMKSC AK+VRRLVF
Sbjct: 66 ADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVIKPTIEGMLGIMKSCAAAKTVRRLVF 125
Query: 483 TSSAGTVNVQEHQQDEYDESSWTDIEFCRTKKMTGWMYFVSKTLAEKAAWEFTERNNIDF 662
TSSAGTVN+QEHQ YDES W+D+EFCR KKMT WMYFVSKTLAE+AAW++ + NNIDF
Sbjct: 126 TSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTAWMYFVSKTLAEQAAWKYAKENNIDF 185
Query: 663 ISIIPTLVVGPFLVPSMPPSLITALSPITGNEPHYSILKQIQLVHLDDLCNAHIYLFEHP 842
I+IIPTLVVGPF++ SMPPSLITALSPITGNE HYSI++Q Q VHLDDLCNAHIYLFE+P
Sbjct: 186 ITIIPTLVVGPFIMSSMPPSLITALSPITGNEAHYSIIRQGQFVHLDDLCNAHIYLFENP 245
Query: 843 EANGRYICSSHNATITDVANLLKQKFPEYSVPTKFEGIDEKLKVVAFSSKRLKDLGFNYK 1022
+A GRYICSSH+ I D+A +L++K+PEY++PT+F+G+DE LK V FSSK+L DLGF +K
Sbjct: 246 KAEGRYICSSHDCIILDLAKMLREKYPEYNIPTEFKGVDENLKSVCFSSKKLTDLGFEFK 305
Query: 1023 YNMADMFVSAVATCRRKGILPLSNQ 1097
Y++ DMF AV TCR KG+LP S++
Sbjct: 306 YSLEDMFTGAVDTCRAKGLLPPSHE 330
>emb|CBI19727.3| unnamed protein product [Vitis vinifera]
Length = 931
Score = 526 bits (1356), Expect = e-147
Identities = 246/325 (75%), Positives = 287/325 (88%)
Frame = +3
Query: 123 ETLCVTGAAGFIGSWLVMRLLERGYVVRATVRDPDNLKKVSHLLELPNAKNKLTLWKADL 302
ET+CVTGA+GFIGSWLVMRLLERGY VRATVRDP N+KKV HLL+LP A+ LTLWKADL
Sbjct: 600 ETVCVTGASGFIGSWLVMRLLERGYTVRATVRDPTNVKKVKHLLDLPKAETHLTLWKADL 659
Query: 303 ADEGSYDDVIKGCTGVFHVATPMDFESKDPENEVIKPTIEGLLSIMKSCVKAKSVRRLVF 482
ADEGS+D+ IKGCTGVFHVATPMDFESKDPENEVIKPTIEG+L IMKSC AK+VRRLVF
Sbjct: 660 ADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVIKPTIEGMLGIMKSCAAAKTVRRLVF 719
Query: 483 TSSAGTVNVQEHQQDEYDESSWTDIEFCRTKKMTGWMYFVSKTLAEKAAWEFTERNNIDF 662
TSSAGTVN+QEHQ YDES W+D+EFCR KKMT WMYFVSKTLAE+AAW++ + NNIDF
Sbjct: 720 TSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTAWMYFVSKTLAEQAAWKYAKENNIDF 779
Query: 663 ISIIPTLVVGPFLVPSMPPSLITALSPITGNEPHYSILKQIQLVHLDDLCNAHIYLFEHP 842
I+IIPTLVVGPF++ SMPPSLITALSPITGNE HYSI++Q Q VHLDDLCNAHIYLFE+P
Sbjct: 780 ITIIPTLVVGPFIMSSMPPSLITALSPITGNEAHYSIIRQGQFVHLDDLCNAHIYLFENP 839
Query: 843 EANGRYICSSHNATITDVANLLKQKFPEYSVPTKFEGIDEKLKVVAFSSKRLKDLGFNYK 1022
+A GRYICSSH+ I D+A +L++K+PEY++PT+F+G+DE LK V FSSK+L DLGF +K
Sbjct: 840 KAEGRYICSSHDCIILDLAKMLREKYPEYNIPTEFKGVDENLKSVCFSSKKLTDLGFEFK 899
Query: 1023 YNMADMFVSAVATCRRKGILPLSNQ 1097
Y++ DMF AV TCR KG+LP S++
Sbjct: 900 YSLEDMFTGAVDTCRAKGLLPPSHE 924
Score = 400 bits (1029), Expect = e-109
Identities = 183/326 (56%), Positives = 248/326 (76%), Gaps = 6/326 (1%)
Frame = +3
Query: 126 TLCVTGAAGFIGSWLVMRLLERGYVVRATVRDPDNLKKVSHLLELPNAKNKLTLWKADLA 305
T+CVTGA+GFIGSWLVM+LL+RGY V ATVRDP N++KV HLLELP A L+LW+ADL
Sbjct: 8 TVCVTGASGFIGSWLVMKLLQRGYYVHATVRDPGNVEKVKHLLELPKASTHLSLWRADLK 67
Query: 306 DEGSYDDVIKGCTGVFHVATPMDFESKDPENEVIKPTIEGLLSIMKSCVKAKSVRRLVFT 485
+EGS+DD I+GC GVFHVA+PMD ++D +NEVI PT+ G+L IM++C KAK+V+R ++T
Sbjct: 68 EEGSFDDAIQGCIGVFHVASPMDISTQDAQNEVIDPTVNGVLDIMRACTKAKTVKRFIYT 127
Query: 486 SSAGTVNV-QEHQQDEYDESSWTDIEFCRTKKMTGWMYFVSKTLAEKAAWEFTERNNIDF 662
S+ GT+ V E EYDES WTD+++C+ +KMT WMYF++KT AEKAAWEF + +D
Sbjct: 128 STTGTITVGPEPLPLEYDESFWTDVDYCKAQKMTAWMYFIAKTTAEKAAWEFAKEKGLDV 187
Query: 663 ISIIPTLVVGPFLVPSMPPSLITALSPITGNEPHYSILKQIQLVHLDDLCNAHIYLFEHP 842
++I P +VVGPF+ PS+PPS L+ +TG E ++L + + VH+DDLC+AHIYLFEHP
Sbjct: 188 VTIQPPVVVGPFVTPSLPPSAKLVLAVLTGEEAGCNLLARGRAVHVDDLCDAHIYLFEHP 247
Query: 843 EANGRYICSSHNATITDVANLLKQKFPEYSVPTKFEGIDEKLKVVAFSSKRLKDLGFNYK 1022
EA GRYICSSH I ++A L K+ EY++PTKFEG+DE LK + SS++L DLG+ +K
Sbjct: 248 EAKGRYICSSHCFNIIELARSLSLKYSEYNIPTKFEGVDESLKSIPCSSRKLLDLGYKFK 307
Query: 1023 YN-----MADMFVSAVATCRRKGILP 1085
YN + D+ A+ +C+ KG++P
Sbjct: 308 YNSEEYDIGDLCSGAIESCKEKGLMP 333
>ref|XP_002281858.1| PREDICTED: dihydroflavonol-4-reductase [Vitis vinifera]
Length = 375
Score = 526 bits (1356), Expect = e-147
Identities = 246/325 (75%), Positives = 287/325 (88%)
Frame = +3
Query: 123 ETLCVTGAAGFIGSWLVMRLLERGYVVRATVRDPDNLKKVSHLLELPNAKNKLTLWKADL 302
ET+CVTGA+GFIGSWLVMRLLERGY VRATVRDP N+KKV HLL+LP A+ LTLWKADL
Sbjct: 44 ETVCVTGASGFIGSWLVMRLLERGYTVRATVRDPTNVKKVKHLLDLPKAETHLTLWKADL 103
Query: 303 ADEGSYDDVIKGCTGVFHVATPMDFESKDPENEVIKPTIEGLLSIMKSCVKAKSVRRLVF 482
ADEGS+D+ IKGCTGVFHVATPMDFESKDPENEVIKPTIEG+L IMKSC AK+VRRLVF
Sbjct: 104 ADEGSFDEAIKGCTGVFHVATPMDFESKDPENEVIKPTIEGMLGIMKSCAAAKTVRRLVF 163
Query: 483 TSSAGTVNVQEHQQDEYDESSWTDIEFCRTKKMTGWMYFVSKTLAEKAAWEFTERNNIDF 662
TSSAGTVN+QEHQ YDES W+D+EFCR KKMT WMYFVSKTLAE+AAW++ + NNIDF
Sbjct: 164 TSSAGTVNIQEHQLPVYDESCWSDMEFCRAKKMTAWMYFVSKTLAEQAAWKYAKENNIDF 223
Query: 663 ISIIPTLVVGPFLVPSMPPSLITALSPITGNEPHYSILKQIQLVHLDDLCNAHIYLFEHP 842
I+IIPTLVVGPF++ SMPPSLITALSPITGNE HYSI++Q Q VHLDDLCNAHIYLFE+P
Sbjct: 224 ITIIPTLVVGPFIMSSMPPSLITALSPITGNEAHYSIIRQGQFVHLDDLCNAHIYLFENP 283
Query: 843 EANGRYICSSHNATITDVANLLKQKFPEYSVPTKFEGIDEKLKVVAFSSKRLKDLGFNYK 1022
+A GRYICSSH+ I D+A +L++K+PEY++PT+F+G+DE LK V FSSK+L DLGF +K
Sbjct: 284 KAEGRYICSSHDCIILDLAKMLREKYPEYNIPTEFKGVDENLKSVCFSSKKLTDLGFEFK 343
Query: 1023 YNMADMFVSAVATCRRKGILPLSNQ 1097
Y++ DMF AV TCR KG+LP S++
Sbjct: 344 YSLEDMFTGAVDTCRAKGLLPPSHE 368