DUS3L_RAT
ID DUS3L_RAT Reviewed; 640 AA.
AC Q3KRC5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like {ECO:0000305};
DE EC=1.3.1.89 {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=mRNA-dihydrouridine synthase DUS3L {ECO:0000305};
DE EC=1.3.1.- {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=tRNA-dihydrouridine synthase 3-like;
GN Name=Dus3l {ECO:0000312|RGD:1563228};
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=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base,
CC in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs
CC (lncRNAs). Mainly modifies the uridine in position 47 (U47) in the D-
CC loop of most cytoplasmic tRNAs. Also able to mediate the formation of
CC dihydrouridine in some mRNAs, thereby regulating their translation.
CC {ECO:0000250|UniProtKB:Q96G46}.
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 -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. {ECO:0000305}.
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DR EMBL; BC105780; AAI05781.1; -; mRNA.
DR RefSeq; NP_001030095.1; NM_001034923.1.
DR AlphaFoldDB; Q3KRC5; -.
DR SMR; Q3KRC5; -.
DR STRING; 10116.ENSRNOP00000066698; -.
DR iPTMnet; Q3KRC5; -.
DR PhosphoSitePlus; Q3KRC5; -.
DR jPOST; Q3KRC5; -.
DR PaxDb; Q3KRC5; -.
DR PRIDE; Q3KRC5; -.
DR GeneID; 301122; -.
DR KEGG; rno:301122; -.
DR CTD; 56931; -.
DR RGD; 1563228; Dus3l.
DR eggNOG; KOG2333; Eukaryota.
DR InParanoid; Q3KRC5; -.
DR OrthoDB; 1016307at2759; -.
DR PhylomeDB; Q3KRC5; -.
DR PRO; PR:Q3KRC5; -.
DR Proteomes; UP000002494; Unplaced.
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:0106414; F:mRNA dihydrouridine synthase activity; ISO:RGD.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
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 InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF01207; Dus; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Flavoprotein; FMN; Isopeptide bond; Metal-binding;
KW mRNA processing; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repeat; tRNA processing; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96G46"
FT CHAIN 2..640
FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like"
FT /id="PRO_0000247344"
FT ZN_FING 110..140
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 148..178
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 301..303
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 355
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 425
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 455
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 487..489
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 510..511
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96G46"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XI1"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96G46"
SQ SEQUENCE 640 AA; 71540 MW; B52A62C52CA00E8E CRC64;
MAEVAEVAAE SGGGGDSGVG ACERGVAPIK AQYRTTKERF HEYLDADKQE GACQETPTEG
PAEPEAKRIR LEDGQENGKT EVAVESHERQ VPKRARGQNK SRPHMKPAHY DKERLCPSLL
QESATPCAFG DRCRFLHDVG RYLETKPADL GPHCVLFNTF GRCPYSMTCR FAGAHLGPEG
QNLVQEEVVA RCAQLPSVRN GLDRALQQQL RKRQVCFERA EQALSHLTQG PMPTIAPEST
VATLTPKHSS CHVQLDNVGG DGARQGSPVP TCGPLTDEDV VRLRPCEKKR LDISGKLYLA
PLTTCGNLPF RRICKRFGAD VTCGEMAMCT NLLQGQMSEW ALLKRHPCED IFGVQLEGAF
PDTMTKCAEL LNRTIDVDFV DINVGCPIDL VYKKGGGCAL MNRSAKFQQI VRGMNEVLDV
PLTVKMRTGV QERVSLAHRL LPELRNWGVA LVTLHGRSRE QRYTRLADWP YIEQCAKVAS
PMPLFGNGDI LSFEDANCAM QTGVAGIMVA RGALLKPWLF TEIKEQRHWD ISSSERLDIL
RDFTHYGLEH WGSDTQGVER TRRFLLEWLS FLCRYVPVGL LERLPQRINE RPPYYLGRDY
LETLMASQQA ADWIRISEML LGPVPPGFVF LPKHKANAYK
