DUS4_SCHPO
ID DUS4_SCHPO Reviewed; 326 AA.
AC O74553;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+];
DE EC=1.3.1.90 {ECO:0000250|UniProtKB:Q06063};
DE AltName: Full=mRNA-dihydrouridine synthase dus4 {ECO:0000305};
DE EC=1.3.1.- {ECO:0000269|PubMed:34798057};
DE AltName: Full=tRNA-dihydrouridine synthase 4;
GN Name=dus4 {ECO:0000303|PubMed:34798057, ECO:0000312|PomBase:SPCC777.15};
GN ORFNames=SPCC777.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34798057; DOI=10.1016/j.molcel.2021.11.003;
RA Finet O., Yague-Sanz C., Krueger L.K., Tran P., Migeot V., Louski M.,
RA Nevers A., Rougemaille M., Sun J., Ernst F.G.M., Wacheul L., Wery M.,
RA Morillon A., Dedon P., Lafontaine D.L.J., Hermand D.;
RT "Transcription-wide mapping of dihydrouridine reveals that mRNA
RT dihydrouridylation is required for meiotic chromosome segregation.";
RL Mol. Cell 0:0-0(2021).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs (PubMed:34798057). Also able to
CC mediate dihydrouridylation of some mRNAs, thereby affecting their
CC translation (PubMed:34798057). {ECO:0000269|PubMed:34798057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53346;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53350;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20b) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20b) in tRNA; Xref=Rhea:RHEA:53352, Rhea:RHEA-COMP:13537,
CC Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53354;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20b) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20b) in tRNA; Xref=Rhea:RHEA:53356, Rhea:RHEA-COMP:13537,
CC Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53358;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
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:0000269|PubMed:34798057};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000269|PubMed:34798057};
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:0000269|PubMed:34798057};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000269|PubMed:34798057};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the Dus family. Dus4 subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA20719.1; -; Genomic_DNA.
DR PIR; T11721; T11721.
DR RefSeq; NP_588262.1; NM_001023252.2.
DR AlphaFoldDB; O74553; -.
DR SMR; O74553; -.
DR BioGRID; 275570; 2.
DR STRING; 4896.SPCC777.15.1; -.
DR MaxQB; O74553; -.
DR PaxDb; O74553; -.
DR EnsemblFungi; SPCC777.15.1; SPCC777.15.1:pep; SPCC777.15.
DR GeneID; 2538996; -.
DR KEGG; spo:SPCC777.15; -.
DR PomBase; SPCC777.15; dus4.
DR VEuPathDB; FungiDB:SPCC777.15; -.
DR eggNOG; KOG2335; Eukaryota.
DR HOGENOM; CLU_013299_4_0_1; -.
DR InParanoid; O74553; -.
DR OMA; FRNCVNT; -.
DR PhylomeDB; O74553; -.
DR PRO; PR:O74553; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
DR GO; GO:0102266; F:tRNA-dihydrouridine20a synthase activity; EXP:PomBase.
DR GO; GO:0102267; F:tRNA-dihydrouridine20b synthase activity; EXP:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IC:PomBase.
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 Flavoprotein; FMN; Mitochondrion; mRNA processing; NAD; NADP;
KW Oxidoreductase; Reference proteome; tRNA processing.
FT CHAIN 1..326
FT /note="tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]"
FT /id="PRO_0000316228"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 26..28
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 149
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 177
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 208..210
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 232..233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
SQ SEQUENCE 326 AA; 37212 MW; 5D2DBF9B6B426BD8 CRC64;
MRDRLKDPVK IFEINKGKRP VHIAAPMVRY SKLPFRQLVR DYNTDIVYTP MILAKEFLHP
KGRYFDFSTN DADASLILQF GVDDPVILEK AAQLVGPYVD GIGINCGCPQ TWAIQEGIGS
ALLDEPEKVH KLVRAVKSTL GESFCTEVKI RIAKDLNKTR HLMQVIEKSG ADIITVHGRT
RQDRSSFPVN LDAIREVRPC VQIPVVANGD VKSLRKGLEI AKYTETQGIM SARGLLENPA
LFAGYEETPW GCVERFLWYS TSYSLNFHLF YHHLTTMMGQ MTTKRERMTI PKDSFASVMD
WLDEHFVVRR PDEPMFGESV LPCRRY
