ID E5A2R5_LEPMJ Unreviewed; 725 AA.
AC E5A2R5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00022143, ECO:0000256|RuleBase:RU291113};
DE EC=1.3.1.89 {ECO:0000256|ARBA:ARBA00012376, ECO:0000256|RuleBase:RU291113};
DE AltName: Full=tRNA-dihydrouridine synthase 3 {ECO:0000256|RuleBase:RU291113};
GN ORFNames=LEMA_P092700.1 {ECO:0000313|EMBL:CBX97861.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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.
CC {ECO:0000256|ARBA:ARBA00033731}.
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:0000256|ARBA:ARBA00033625};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366;
CC Evidence={ECO:0000256|ARBA:ARBA00033625};
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:0000256|ARBA:ARBA00033656};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362;
CC Evidence={ECO:0000256|ARBA:ARBA00033656};
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:0000256|ARBA:ARBA00033653};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
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:0000256|ARBA:ARBA00033638};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|RuleBase:RU291113};
CC -!- SIMILARITY: Belongs to the dus family. Dus3 subfamily.
CC {ECO:0000256|RuleBase:RU291113}.
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DR EMBL; FP929132; CBX97861.1; -; Genomic_DNA.
DR RefSeq; XP_003841340.1; XM_003841292.1.
DR AlphaFoldDB; E5A2R5; -.
DR STRING; 985895.E5A2R5; -.
DR EnsemblFungi; CBX97861; CBX97861; LEMA_P092700.1.
DR GeneID; 13281305; -.
DR eggNOG; KOG2333; Eukaryota.
DR HOGENOM; CLU_013299_7_0_1; -.
DR InParanoid; E5A2R5; -.
DR OMA; WSYIAEC; -.
DR OrthoDB; 275918at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102265; F:tRNA-dihydrouridine47 synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 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 PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR Pfam; PF01207; Dus; 2.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU291113};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU291113};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723,
KW ECO:0000256|RuleBase:RU291113};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU291113};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU291113};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU291113};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|RuleBase:RU291113};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723, ECO:0000256|RuleBase:RU291113};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 129..162
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 129..162
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81507 MW; B7DFF8B6A2956DC9 CRC64;
MTTEAMEGVV KDEPVPNGAP VESHGTAYSG NGGEVDANAE KKRARSSTPV HDETSVKRVK
GVAPIKAEFL IHRGDNRIAT KEKVVDDDAA EAADDRYRKD ARDGGGNGKG KKDKKQRGQN
TSRNFGSSRD KTPLCSSRAL FNEFSAKECP FGQKCKFEHD LRRYLREGRR EDLTTMNGQC
PVFEVKGFCH MGWKCRFVGS HSEERTTEDG RKELVLKEDA ERKAQVADVE EEVGVVNIVS
KDVKFGLSRR KISTPRSDQY IEWIEKNKGL EREVFDSTMG DSKALKEELE ARRAEYVEAP
FRPSEKRRIY YGPETPVLAP LTTQGNMPYR RLCVDLGCQV TWSEMAMGMP LIQGERGEWA
LMKAHESEIT PPAFQSKNKV VQGYDNSTDM KFGAQIAANK PWLATKTVEV LTDHCPKLRA
IDLNCGCPIN LVCEKGAGSA LLDQEAKLEQ ILRGMNYVSK EVPITVKIRM GTKDNQPTAQ
KLIKRLVLGG RESIETGKGT CGIAAITLHG RSKQQRYSRS ADWSYIAECA SLITRLKKER
DAQIDTLAEP DARDQPNGGT VYFVGNGDCY SHTDYYNALD SAHVDSVMIG RGALIKPWIF
EEITTNQYLD KSATERLAYI EKFAKYGMQT WGSDEQGIGT TRRFMLEWLS FAHRYVPVGI
LEYLPPHIQD RPPIFKGRNE LETLLASEHY KDWIKLSEMF LGPAHPNFKF EPKHKSNAYE
IEAEG
//
