ID DUS3_PICST Reviewed; 613 AA. AC A3LUK5; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]; DE EC=1.3.1.89; DE AltName: Full=tRNA-dihydrouridine synthase 3; GN Name=DUS3; ORFNames=PICST_83606; OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / OS NRRL Y-11545) (Yeast) (Pichia stipitis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; OC Scheffersomyces. OX NCBI_TaxID=322104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose- RT fermenting yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified CC base found in the D-loop of most tRNAs. Specifically modifies U47 CC in cytoplasmic tRNAs (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(47) in tRNA + NAD(P)(+) = CC uracil(47) in tRNA + NAD(P)H. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000250|UniProtKB:Q5SMC7}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000498; ABN66252.1; -; Genomic_DNA. DR RefSeq; XP_001384281.1; XM_001384244.1. DR ProteinModelPortal; A3LUK5; -. DR STRING; 322104.XP_001384281.1; -. DR EnsemblFungi; ABN66252; ABN66252; PICST_83606. DR GeneID; 4838835; -. DR KEGG; pic:PICST_83606; -. DR eggNOG; KOG2333; Eukaryota. DR eggNOG; COG0042; LUCA. DR HOGENOM; HOG000240610; -. DR InParanoid; A3LUK5; -. DR KO; K05544; -. DR OMA; WALMKAH; -. DR OrthoDB; EOG092C20WI; -. DR Proteomes; UP000002258; Chromosome 4. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0102265; F:tRNA-dihydrouridine47 synthase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Flavoprotein; FMN; Metal-binding; NAD; KW NADP; Nucleus; Oxidoreductase; Reference proteome; Repeat; KW tRNA processing; Zinc; Zinc-finger. FT CHAIN 1 613 tRNA-dihydrouridine(47) synthase FT [NAD(P)(+)]. FT /FTId=PRO_0000330247. FT ZN_FING 88 111 C3H1-type 1. FT ZN_FING 128 149 C3H1-type 2. FT NP_BIND 250 252 FMN. {ECO:0000250|UniProtKB:Q5SMC7}. FT NP_BIND 456 458 FMN. {ECO:0000250|UniProtKB:Q5SMC7}. FT NP_BIND 480 481 FMN. {ECO:0000250|UniProtKB:Q5SMC7}. FT ACT_SITE 337 337 Proton donor. FT {ECO:0000250|UniProtKB:Q5SMC7}. FT BINDING 305 305 FMN. {ECO:0000250|UniProtKB:Q5SMC7}. FT BINDING 377 377 FMN. {ECO:0000250|UniProtKB:Q5SMC7}. FT BINDING 408 408 FMN. {ECO:0000250|UniProtKB:Q5SMC7}. SQ SEQUENCE 613 AA; 69682 MW; 2F1C257CCA755FB8 CRC64; MTAGEKRTSE ALDQPESKKV HVERGMAAIK PEFIVQKDRI VDSFDDDEAE GGERGVEEGK SGKGGKKKRR GQNKNRDLKQ KREEIRLCTS LLDPDNIKTC AYGPEQCRST HNVEEYLASK PVDIEGICPV FRAIGYCPAG LKCRWLQSHY DKETRKLIKD LGRTEASKIE LNYEVNNVSH EARGKLRKKQ YDFAIAGKVI EYIDSTVQND ENIANAKEQR KNNEATYVDA PYKIAEKKRL DFRNAKIVSP LTTVGNLPYR RLMKKLGADI TYSEMALSVP LLQATNAEWA LPKAHRTEYP GYGVQIATSK HWAAAKVAEI ISRETEHVSE LNLNCGCPID LLYRQGQGSA LLEQPARLVR ILKAMNASSG DIPVTVKIRT GSKENKNTAK TLVERLLAEN DVAAITLHGR SRQQRYTKEA DWNYIAEVGQ VVQQWNDKKE ENKDSRDTQR TCFVGNGDVF SHVDWYNAVN TDGIDSVMVA RGALIKPWIF EEVEAQQYLD KTATERLDIL KTFSDYALEH WGTDEYGVGL ARRFMCEFLS FTHRYIPLGI LERLPPKINE RPPQWKGRNE METLLGSTDY KDWIKITEMF LGKSGDDFVF TPKHKSNSYE KSN //