DUS2_YEAST
ID DUS2_YEAST Reviewed; 384 AA.
AC P53720; D6W1J0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=tRNA-dihydrouridine(20) synthase [NAD(P)+];
DE EC=1.3.1.91 {ECO:0000269|PubMed:12003496};
DE AltName: Full=mRNA-dihydrouridine synthase DUS2 {ECO:0000305};
DE EC=1.3.1.- {ECO:0000250|UniProtKB:O74731};
DE AltName: Full=tRNA-dihydrouridine synthase 2;
GN Name=SMM1; Synonyms=DUS2 {ECO:0000303|PubMed:12003496};
GN OrderedLocusNames=YNR015W; ORFNames=N2065;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R100;
RA Rinaldi T., Lande R., Bolotin-Fukuhara M., Frontali L.;
RT "Identification of three nuclear genes which in high copy number suppress a
RT mitochondrial mutation in the tRNA(Asp) gene in Saccharomyces cerevisiae.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12003496; DOI=10.1017/s1355838202029825;
RA Xing F., Martzen M.R., Phizicky E.M.;
RT "A conserved family of Saccharomyces cerevisiae synthases effects
RT dihydrouridine modification of tRNA.";
RL RNA 8:370-381(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=14970222; DOI=10.1074/jbc.m401221200;
RA Xing F., Hiley S.L., Hughes T.R., Phizicky E.M.;
RT "The specificities of four yeast dihydrouridine synthases for cytoplasmic
RT tRNAs.";
RL J. Biol. Chem. 279:17850-17860(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs (PubMed:12003496, PubMed:14970222).
CC Specifically modifies U20 in cytoplasmic tRNAs (PubMed:12003496,
CC PubMed:14970222). Also able to mediate dihydrouridylation of some
CC mRNAs, thereby affecting their translation (By similarity).
CC {ECO:0000250|UniProtKB:O74731, ECO:0000269|PubMed:12003496,
CC ECO:0000269|PubMed:14970222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20) in tRNA; Xref=Rhea:RHEA:53336, Rhea:RHEA-COMP:13533,
CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC Evidence={ECO:0000269|PubMed:12003496};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53338;
CC Evidence={ECO:0000269|PubMed:12003496};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533,
CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC Evidence={ECO:0000269|PubMed:12003496};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53342;
CC Evidence={ECO:0000269|PubMed:12003496};
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:O74731};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000250|UniProtKB:O74731};
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:O74731};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000250|UniProtKB:O74731};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 2650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Dus family. Dus2 subfamily. {ECO:0000305}.
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DR EMBL; X91816; CAA62924.1; -; Genomic_DNA.
DR EMBL; Z71630; CAA96293.1; -; Genomic_DNA.
DR EMBL; Z71631; CAA96295.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10556.1; -; Genomic_DNA.
DR PIR; S63345; S63345.
DR RefSeq; NP_014412.1; NM_001183192.1.
DR AlphaFoldDB; P53720; -.
DR SMR; P53720; -.
DR BioGRID; 35840; 82.
DR DIP; DIP-4102N; -.
DR STRING; 4932.YNR015W; -.
DR iPTMnet; P53720; -.
DR MaxQB; P53720; -.
DR PaxDb; P53720; -.
DR PRIDE; P53720; -.
DR EnsemblFungi; YNR015W_mRNA; YNR015W; YNR015W.
DR GeneID; 855749; -.
DR KEGG; sce:YNR015W; -.
DR SGD; S000005298; SMM1.
DR VEuPathDB; FungiDB:YNR015W; -.
DR eggNOG; KOG2334; Eukaryota.
DR GeneTree; ENSGT00550000075019; -.
DR HOGENOM; CLU_013299_3_2_1; -.
DR InParanoid; P53720; -.
DR OMA; HWSSTKF; -.
DR BioCyc; MetaCyc:G3O-33331-MON; -.
DR BioCyc; YEAST:G3O-33331-MON; -.
DR BRENDA; 1.3.1.91; 984.
DR PRO; PR:P53720; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53720; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IDA:SGD.
DR GO; GO:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IDA:SGD.
DR GO; GO:0008033; P:tRNA processing; IGI:SGD.
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; DUS_fam.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Flavoprotein; FMN; Glycoprotein; mRNA processing; NAD; NADP;
KW Nucleus; Oxidoreductase; Reference proteome; tRNA processing.
FT CHAIN 1..384
FT /note="tRNA-dihydrouridine(20) synthase [NAD(P)+]"
FT /id="PRO_0000162154"
FT REGION 359..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 12..14
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 88
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 160
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 188
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 222..224
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 249..250
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
SQ SEQUENCE 384 AA; 42816 MW; 637EEC05DD4F9D6D CRC64;
MVTYAGKLVL APMVRAGELP TRLMALAHGA DLVWSPEIID KKLIQCVRKE NTALQTVDYV
VPSKVQTRPE TLVFRTYPKL ESSKLIFQIG SASPALATQA ALKVINDVSG IDINAGCPKH
FSIHSGMGSA LLRTPDTLCL ILKELVKNVG NPHSKPISVK IRLLDTKQDT LQLVKRLCAT
GITNLTVHCR KTEMRNREQP ITDYIAEIYE ICQANNVSLI VNGAIRDRSH FHDLQANHWK
NTNIGGMIAE CAERDPTVFD HTSKPSEDGP SWVVACREFI QWATKFDNHI GNTKYMLSRI
VPGKSVFFQY FARCKSPEEV SFVLKQLNDD GSAQTDPSEY LENCRAQEKA LKNANAIAKQ
KRKQTDHIGS DTKKQKVVPL PTDI
