ID A0A2U1N917_ARTAN Unreviewed; 1062 AA.
AC A0A2U1N917;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cinnamoyl-CoA reductase 1 {ECO:0000313|EMBL:PWA69999.1};
DE SubName: Full=Dihydroflavonol reductase {ECO:0000313|EMBL:QGV13662.1};
GN Name=DFR {ECO:0000313|EMBL:QGV13662.1};
GN ORFNames=CTI12_AA292570 {ECO:0000313|EMBL:PWA69999.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA69999.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA69999.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA69999.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
RN [2] {ECO:0000313|EMBL:QGV13662.1}
RP NUCLEOTIDE SEQUENCE.
RA Hassani D.;
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000256|ARBA:ARBA00005690}.
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DR EMBL; PKPP01003322; PWA69999.1; -; Genomic_DNA.
DR EMBL; MK948609; QGV13662.1; -; mRNA.
DR AlphaFoldDB; A0A2U1N917; -.
DR STRING; 35608.A0A2U1N917; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08958; FR_SDR_e; 2.
DR CDD; cd04480; RPA1_DBD_A_like; 1.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR047192; Euk_RPA1_DBD_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR003871; RPA1_DBD-A-like_plant.
DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR PANTHER; PTHR10366:SF825; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN; 1.
DR Pfam; PF02721; DUF223; 1.
DR Pfam; PF01370; Epimerase; 2.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
PE 2: Evidence at transcript level;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245207};
KW Zinc {ECO:0000256|ARBA:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 7..220
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT DOMAIN 291..531
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT DOMAIN 667..753
FT /note="RPA1 ssDNA-binding"
FT /evidence="ECO:0000259|Pfam:PF02721"
FT DOMAIN 850..979
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
FT REGION 1016..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 116994 MW; 5D29EC139090DA5B CRC64;
MLLIEEYSYV AADPKKTEHL VALDGAKERL TLFEATLTEE GSFDAAIDGC VCVFHTASPV
LLSVDDPHAQ LVDPAVKGTL SVLKSAAKVP SLKRVVLTSS MAAVVFGAKL PEPSDVVDET
WFSDPVLCEQ KKLWYMLSKT LAEDAAVKFS RENGLELVAI NPGYVIGPIL QPTLNMTSEG
FMRMIETGQG VFADGIYRLV DVRDVAMAHI LAFENPEANG RYCVVGKVIH SSDIMKIVAK
LYPTLGHSKG YTDGKDAEPQ FYSVSRVKAE GLGVEFTPVE HQTMSGEGKV VCVTGASGFI
ASWLVKLLLA RGYSVVATVR SLGDPKKTEH LLALDGAKER LSLFEANLIE DGSFDSAVKG
CVCVFHTASP VQFIVDDPQA QLIDPAVKGT LNVLNSASKV PSLRRVVLTS SMASVLFGAK
VPVFGDVVDE TWFSDPTVCQ KRNSWYCVSK TMAEDAAVKF SQENDMDLVV INPGFVIGPI
LQPTLNNTSK RFMNFIKTGE DVFSDRVYIL VDVRDVAIAH ILAFEKPEAN GRYCVVGNVS
SEIMKIVEKL YPTIDHSRRY KDSKGVESLI YSVSRVKTEG LGVEFTPLEV GTCAGEESVG
PRNGGSGAWV GLDYLISVAR LGGQPALGCG GYINDLSAVK DNIKLRVRIV RSWMQDVYGK
QGIKNMELVL MDEQSAKMQA TVRMALVNGF KHKLEEGSAV TLSRYSLGDI QPKYRMVNKP
LRLSFLSNTI IEPCPDFTGS IYVFDFRAFK TITDLQQEED GQFDVIGHVV ACDDLDNYDK
NGRSGKKKPL TLADAELFAD KDQAKSDNTA SRISTQSRHS TRDEFLNKLQ FKNIVELLDV
DQGKASVIVG TVIAIHEEEG WWYLGCRKCN KKVVKESQFV DLETETKNKF GYQTANEWRC
TKCDVIVTGI KTEYRLQLRV QDESGTISLS LFNDEVQAMV GRSAYQLCDK YGCKNAEDQN
FPKEITNLVG KRYAFKVAID EVNAKKLLPV FTVLRLTDDS DILNSIVSTV TPVKDLESQT
DENTTPVENQ NSGKRASDVE RETDGSSIKR QLLDIKMEKA AK
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