DUS1L_RAT
ID DUS1L_RAT Reviewed; 438 AA.
AC Q8K582;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like;
DE EC=1.3.1.88 {ECO:0000250|UniProtKB:Q6P1R4};
DE AltName: Full=Liver regeneration-related protein LRRG08/LRRG09;
DE AltName: Full=tRNA-dihydrouridine synthase 1-like;
GN Name=Dus1l; Synonyms=Pp3111;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) 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. {ECO:0000250|UniProtKB:Q6P1R4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SIMILARITY: Belongs to the Dus family. Dus1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF508021; AAM34683.1; -; mRNA.
DR EMBL; AY327509; AAP97740.1; -; mRNA.
DR EMBL; AY327510; AAP97741.1; -; mRNA.
DR RefSeq; NP_742015.1; NM_172018.1.
DR AlphaFoldDB; Q8K582; -.
DR SMR; Q8K582; -.
DR STRING; 10116.ENSRNOP00000067257; -.
DR PhosphoSitePlus; Q8K582; -.
DR PaxDb; Q8K582; -.
DR GeneID; 246185; -.
DR KEGG; rno:246185; -.
DR CTD; 64118; -.
DR RGD; 708389; Dus1l.
DR eggNOG; KOG2335; Eukaryota.
DR InParanoid; Q8K582; -.
DR OrthoDB; 1318230at2759; -.
DR PhylomeDB; Q8K582; -.
DR PRO; PR:Q8K582; -.
DR Proteomes; UP000002494; Unplaced.
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:0002943; P:tRNA dihydrouridine synthesis; ISS:UniProtKB.
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; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; NAD; NADP; Oxidoreductase; Reference proteome;
KW tRNA processing.
FT CHAIN 1..438
FT /note="tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-
FT like"
FT /id="PRO_0000247228"
FT REGION 343..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 23..25
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 147
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 175
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 438 AA; 49709 MW; 9C13F8681D3BD194 CRC64;
MPKLQGFEFW SRALGGARHV VAPMVDQSEL AWRLLSRRHG AQLCYTPMLH AQVFVRDANY
RKENLYCDVC PEDRPLIVQF CANDPEVFVQ AALLAQDYCD AIDLNLGCPQ MIAKRGRYGA
FLQEEWDLLQ RMILLAHERL SVPVTCKIRV FPEIDKTVRY AQMLEKAGCQ LLTVHGRTKE
QKGPMAGTAS WEHIKAVRKA VGIPVFANGN IRCLQDVERC IQDTGVQGVM SAEGNLHNPA
LFEGRSPAVW ELADEYLDIV RQHPCPLSYV RAHLFKLWHH TLQVHQQLRE ELAKVKTLEG
VAAVSQALKL RCQEDMARQQ EGVRPADNLP AFHWICQPYI RPGPKEGSKE NSSGRSKRAL
EEEEGSMEGL SKNKLKKQLR NPHKTFDPSL KPKYAKCDQC GNPKGNRCVF NLCRGCCKKR
AFRETADCPG HDCFLRPN
