DUS3L_DICDI
ID DUS3L_DICDI Reviewed; 671 AA.
AC Q54CU9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like;
DE EC=1.3.1.89 {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=mRNA-dihydrouridine synthase dus3l;
DE EC=1.3.1.- {ECO:0000250|UniProtKB:Q9UTH9};
DE AltName: Full=tRNA-dihydrouridine synthase 3-like;
GN Name=dus3l; ORFNames=DDB_G0292686;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. Specifically modifies U47 in
CC cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of
CC dihydrouridine in some mRNAs, thereby affecting their translation (By
CC similarity). {ECO:0000250|UniProtKB:Q06053,
CC ECO:0000250|UniProtKB:Q9UTH9}.
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; AAFI02000194; EAL61146.1; -; Genomic_DNA.
DR RefSeq; XP_629571.1; XM_629569.1.
DR AlphaFoldDB; Q54CU9; -.
DR SMR; Q54CU9; -.
DR STRING; 44689.DDB0238072; -.
DR PaxDb; Q54CU9; -.
DR EnsemblProtists; EAL61146; EAL61146; DDB_G0292686.
DR GeneID; 8628832; -.
DR KEGG; ddi:DDB_G0292686; -.
DR dictyBase; DDB_G0292686; dus3l.
DR eggNOG; KOG2333; Eukaryota.
DR HOGENOM; CLU_013299_7_0_1; -.
DR InParanoid; Q54CU9; -.
DR OMA; KHNANAY; -.
DR PhylomeDB; Q54CU9; -.
DR PRO; PR:Q54CU9; -.
DR Proteomes; UP000002195; Chromosome 6.
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:dictyBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; ISS:dictyBase.
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 SMART; SM00356; ZnF_C3H1; 2.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; Metal-binding; mRNA processing; NAD; NADP;
KW Oxidoreductase; Reference proteome; Repeat; tRNA processing; Zinc;
KW Zinc-finger.
FT CHAIN 1..671
FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like"
FT /id="PRO_0000346796"
FT ZN_FING 99..127
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 134..164
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 39..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 330..332
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 384
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 484
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 515..517
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 539..540
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
SQ SEQUENCE 671 AA; 76229 MW; 3216201B25664FA8 CRC64;
MESVETTTPS NSEIKSVETI VEEQKVNETN TTLNAEVVET PTKTEEKSKT EITNENKERS
RGLEAKIKPE FVLPFKKIEK VEVDKAAKKK EFRNQLRESM NDKLCPKISK GLVCEFNETC
KFSHDVEKYL ASKPKSIGIC QNFQTYGECK YGLNCYFGEC HIVDNKTIVN KELIGKVEPV
KTLNEVSNEI QIQLKTNNYP FPKSEIYFNE NGISVRQIKG RNNNNNKNNN KQNDNKRKEN
EKDDDDDKLN KKIKLENENT TTTTTTTTTT TTETTEKTEK TEKTEKTETT ETKKEEFKQS
NENTEIDIMT PLKANEKKRI NFENQLILAP LTTVGNLPFR RICKRLGADI TIGEMALTTK
LLEGTKSELA LLKRHPCEDK FGVQICGSYV DAAVKCAEFI ENEIDADFVD INSGCPIDLV
CNMGAGAALM ERPKKVEQLL RGISSSLSCP TTIKIRIGKS EDAPTAHKLI PSLGEWGACA
VTLHGRSRAQ RYSRLANWDY VKQCSEVSSI PLIGNGDIYN YQDVVNIYDS SKVSSIMIAR
GALIKPWIFT EIKEKREWDI SASERLDFIR DFANYGLDHW GSDRIGVDNT RKFLLNWLSF
SHRYIPVGLL DKVHYMNERP PAYFGRSDLE TLLASTQVKD WIKITEMFLG PVTSDYSFVP
KHNSNSYESQ G
