(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 99.
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; 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). {ECO:0000250}.
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   -!- 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   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. {ECO:0000305}.
DR   EMBL; AE016818; AAS52754.1; -; Genomic_DNA.
DR   RefSeq; NP_984930.1; NM_210284.1.
DR   STRING; 33169.AAS52754; -.
DR   EnsemblFungi; AAS52754; AAS52754; AGOS_AER070C.
DR   GeneID; 4621133; -.
DR   KEGG; ago:AGOS_AER070C; -.
DR   HOGENOM; HOG000240610; -.
DR   InParanoid; Q757E3; -.
DR   KO; K05544; -.
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   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; IPR001269; tRNA_hU_synthase.
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;
DR   PRODOM; Q757E3.
DR   SWISS-2DPAGE; Q757E3.
KW   Cytoplasm; Flavoprotein; FMN; Metal-binding; NAD; NADP; Nucleus;
KW   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   NP_BIND         281..283
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   NP_BIND         489..491
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   NP_BIND         513..514
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   ACT_SITE        369
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         336
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         409
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         440
FT                   /note="FMN"
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
//

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