DUS3L_XENTR
ID DUS3L_XENTR Reviewed; 639 AA.
AC Q28BT8; Q6P2X3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 80.
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; ORFNames=TNeu105e03.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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; CR942642; CAJ83250.1; -; mRNA.
DR EMBL; BC064263; AAH64263.1; -; mRNA.
DR RefSeq; NP_989334.1; NM_204003.1.
DR AlphaFoldDB; Q28BT8; -.
DR SMR; Q28BT8; -.
DR STRING; 8364.ENSXETP00000057164; -.
DR PaxDb; Q28BT8; -.
DR GeneID; 394959; -.
DR KEGG; xtr:394959; -.
DR CTD; 56931; -.
DR Xenbase; XB-GENE-943237; dus3l.
DR eggNOG; KOG2333; Eukaryota.
DR InParanoid; Q28BT8; -.
DR OrthoDB; 1016307at2759; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; 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: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; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF01207; Dus; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; Metal-binding; mRNA processing; NAD; NADP;
KW Oxidoreductase; Reference proteome; Repeat; tRNA processing; Zinc;
KW Zinc-finger.
FT CHAIN 1..639
FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like"
FT /id="PRO_0000247346"
FT ZN_FING 122..152
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 160..190
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 385
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 300..302
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 354
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 424
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 454
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 486..488
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 509..510
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT CONFLICT 13
FT /note="N -> T (in Ref. 1; CAJ83250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 72480 MW; B65DA16A93C98187 CRC64;
MAESDGSNNE NGNLDTVTQK LDRGVAAIKP QYLTTKEKFH VFIDADGKEV VDKQTCSELS
GNDAENTVRA EDAAEPEAKR IKLDDGTGEG QDKPPTSAEN KQEKKRARGQ NKSRPHMKHS
QFEENKLCPS VTQECASKCF FGDKCKFLHD VAKYVSEKPE DIRPNCYLYE TFGKCIYGVT
CRFAKSHLGD NFKNLINEEL MKQWEGQVLV KNSLDKSLKE QLRKRKVVFE KTDKYLKLCN
KSGDSLKIKS PVVKEDNAAQ VVQKDSPVTT VGAVTDEDLV KLRPCEKKTI DFRNKLYLAP
LTTCGNLPFR RLCKRFGADI TCGEMAMCTN LLQGQPSEWA LLKRHHSEDI FGVQLEGAFP
DTMTKCAELL NRTIDVDFVD INVGCPIDLV YKKGGGCGLM NRTNKFEQIV KGMNSVLDVP
LTVKIRTGVQ EKINIAHKLI PNLRDWGVSL VTLHGRSREQ RYTKLADWEY IAQCADIASP
LPLFGNGDII SYEDANRALQ TGVSGIMLAR GALLKPWLFT EIKEQRHWDI SSTERFDILK
DFTNYGLEHW GSDCQGVEKT RRFMLEWLSF LCRYIPIGLL EHVPQKINER PPYYMGRDYM
ETLMASQNVT DWIKISEMLL GPVPPNFSFL PKHKANSYK
