DUS3_ASHGO
ID DUS3_ASHGO Reviewed; 647 AA.
AC Q757E3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)];
DE EC=1.3.1.89 {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=mRNA-dihydrouridine synthase DUS3;
DE EC=1.3.1.- {ECO:0000250|UniProtKB:Q9UTH9};
DE AltName: Full=tRNA-dihydrouridine synthase 3;
GN Name=DUS3; OrderedLocusNames=AER070C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. Specifically modifies U47 in
CC cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of
CC dihydrouridine in some mRNAs, thereby affecting their translation (By
CC similarity). {ECO:0000250|UniProtKB:Q06053,
CC ECO:0000250|UniProtKB:Q9UTH9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(47) in tRNA; Xref=Rhea:RHEA:53364, Rhea:RHEA-COMP:13539,
CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(47) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(47) in tRNA; Xref=Rhea:RHEA:53360, Rhea:RHEA-COMP:13539,
CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06053}. Nucleus
CC {ECO:0000250|UniProtKB:Q06053}.
CC -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. {ECO:0000305}.
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DR EMBL; AE016818; AAS52754.1; -; Genomic_DNA.
DR RefSeq; NP_984930.1; NM_210284.1.
DR AlphaFoldDB; Q757E3; -.
DR SMR; Q757E3; -.
DR STRING; 33169.AAS52754; -.
DR PRIDE; Q757E3; -.
DR EnsemblFungi; AAS52754; AAS52754; AGOS_AER070C.
DR GeneID; 4621133; -.
DR KEGG; ago:AGOS_AER070C; -.
DR eggNOG; KOG2333; Eukaryota.
DR HOGENOM; CLU_013299_7_0_1; -.
DR InParanoid; Q757E3; -.
DR OMA; IAANKPW; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
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:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
DR GO; GO:0102265; F:tRNA-dihydrouridine47 synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF01207; Dus; 1.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Flavoprotein; FMN; Metal-binding; mRNA processing; NAD; NADP;
KW Nucleus; Oxidoreductase; Reference proteome; Repeat; tRNA processing; Zinc;
KW Zinc-finger.
FT CHAIN 1..647
FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]"
FT /id="PRO_0000330225"
FT ZN_FING 86..116
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 122..158
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 369
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 281..283
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 336
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 409
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 440
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 489..491
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 513..514
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
SQ SEQUENCE 647 AA; 73220 MW; DF0732DBA7EF8E35 CRC64;
MSSTEGGAKR VAEDGSEVSE AKRVGRIEGV AQLKPEYVVA GAAQLRAAES DEELTSERMV
EPEGGTRKKS KKARGQNKNR DNRQAKEEHQ LCPRLAQGNA DACAFGAQCR YLHDVRTYLE
HKTAEIECPQ FTGCPVFAAT GRCPMGFKCR FLSSHCNMET LELATTPEDE RAKLWSVNHE
VNHIASDRKL DLVKRRAPFP RSEHVLEIID AIQQEFRDEM QGAAAAPEGA VAEVPQVQQR
EEQLSNKRAR QRELYAQYHE TRYFAQEKKP LDLHHKKIVS PLTTVGNLPF RRLMRQLGAD
VTYSEMALAV PLIQGTNSEW ALPKAHCSEL PGFGVQLACS KPWQAAKAAE ALADNVGDGL
SEINLNSGCP IDLLYRQGSG SALLDNPARM IRCLNAMNYV SKDVPVSVKL RTGTRDGHPI
ALGLCKRLVM ETDVAAITLH GRTRQQRYTR SADWDYVGQV ADALRSYETE RAEKLKDREG
KLRIQFVGNG DCNNWEDWYR HLENENVDSV MVARGALIKP WIFEEVDARQ YIDKSSSERL
EILRDYARFS MDHWGTDEYG IALCRRYFCE FMSFFHRYVP MGICERYPVL LNERPPNWRG
RDDLETLLGS TDAADWIKLS EQFFGPTPDK FVFQPKHKSN SYAPSVQ
