DUS3_USTMA
ID DUS3_USTMA Reviewed; 867 AA.
AC Q4P1U2; A0A0D1DUB7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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; ORFNames=UMAG_05921;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003159; KIS66185.1; -; Genomic_DNA.
DR RefSeq; XP_011392257.1; XM_011393955.1.
DR AlphaFoldDB; Q4P1U2; -.
DR SMR; Q4P1U2; -.
DR STRING; 5270.UM05921P0; -.
DR EnsemblFungi; KIS66185; KIS66185; UMAG_05921.
DR GeneID; 23565671; -.
DR KEGG; uma:UMAG_05921; -.
DR VEuPathDB; FungiDB:UMAG_05921; -.
DR eggNOG; KOG2333; Eukaryota.
DR HOGENOM; CLU_013299_7_1_1; -.
DR InParanoid; Q4P1U2; -.
DR OMA; RRFMCEM; -.
DR OrthoDB; 1016307at2759; -.
DR Proteomes; UP000000561; Chromosome 20.
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: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 Pfam; PF01207; Dus; 2.
DR PROSITE; PS01136; UPF0034; 1.
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..867
FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]"
FT /id="PRO_0000330249"
FT ZN_FING 149..173
FT /note="C3H1-type 1"
FT ZN_FING 278..299
FT /note="C3H1-type 2"
FT REGION 71..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 583
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 496..498
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 550
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 623
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 653
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 704..706
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 728..729
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
SQ SEQUENCE 867 AA; 95008 MW; 6E83BB5CBF9A4941 CRC64;
MSEADAATSA MDSAAEAAEQ VWKHPVYGAT DKYTPGIAPI KAEYILPKPA SGSVAVVEVN
DDASERLTKR ALATTGDSAS VTTNTSDEAP KKLKGAARKR ARREEAAALA AAHRAEKKCK
AGQQTQHAKK GGQNKARQFS SLKDAHGHCH GFLSRGVQGC KFAQCAQACR FSHDLVSYLE
KKERDLFLPA VPHKQLDAMS HTQKMQWLQD SYSLTLLPAS NTSTTASAST QQLEAQQQAQ
GEMTTFVRAS SSAAVPPRSD LPASSDPAHA SLDWSTTCPI FAVKGFCTMG WKCRFLGSHV
RLVGASSLGD PLNPTGFASS GLELVRDQAR MDEWRARTRA FELSHAKQSA SDADQDELNF
GTSDGMKAMR KRNFPLPKTK AVLKFLETET KQLADVDPHG SIAGKGPIPT SVVEEAVAVS
AGANGCNGHS TAPASAAAAE AEAEDDLEEL ENAMRNRGLH ARVAQAATTN GSIDLARIRP
SEKRRLNWRG ELYLAPLTTT GNLPFRRICT GYGSDIHCGE MGLAESFLHG NAAEWSLVRR
HESERIFGTQ LCGGKPDLLV PVAEALKAEV GDGLDFVDIN CGCPIDLVFN KGAGSALLDH
PTKLSKIVRG MNAVLGDTPL TIKLRTGTGA KQTTHKIFAK AQTEWRVAAA TLHGRSRKQR
YKNDADWGYI ATCANTLRES VSEWNESSRF ADEPEMVPIP VYGNGDVYSW QDYYERIERT
HVDGEMIARG ALIKPWLFTE IKERRDWDIS SRERLDMMRK FAEYGLTHWG SDTHGVNTTR
RFMCEMMSFT HRYVPTGLLE FLPSRLNDRP PLFRGRDELE TLLASSNAQD WVKLTEMFLG
KPPQEWSFTP KHKSSSYSTD DAAEQQG
