ID A0A0F9XF30_TRIHA Unreviewed; 766 AA.
AC A0A0F9XF30;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00022143};
DE EC=1.3.1.89 {ECO:0000256|ARBA:ARBA00012376};
DE AltName: Full=tRNA-dihydrouridine synthase 3 {ECO:0000256|ARBA:ARBA00031322};
GN ORFNames=THAR02_04752 {ECO:0000313|EMBL:KKP03130.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP03130.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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 -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005451}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKP03130.1}.
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DR EMBL; JOKZ01000122; KKP03130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9XF30; -.
DR OMA; WSYIAEC; -.
DR OrthoDB; 275918at2759; -.
DR Proteomes; UP000034112; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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 InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
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.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 359..569
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT DOMAIN 606..656
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 86149 MW; 79DF140087417C61 CRC64;
MNGQHPDVDS QPEERAAKRI KIDDAGAAQD HKGENGQETA QVPQNGNHVE HSDNQGQSVP
EASNPSEESG EPADRVKGMA PIKKEYLIDM SGKQNERSAA VDDDAAEGRG SNDRDQRDGQ
DARDRGKKGK KKAKGQNIDR SFGRFDDAIP LCNSRAYSAE FSPKECQYGD GCKMCHDLRK
YLSEGRREDV EALGGKCPAF EAYGYCASGW KCRFVKSHMQ EIEHADGRKE LVLSDNRPSK
VEHKEPPKEE ESAPLETSEE KGSKFEERRK SEDELRPGIF NVVTMGQKIE LNRKRLDFTK
ADEYIKWLNH EAGISQDFHH RRKDQPALGL EDLRARFVDP PFKPSEKRRL YFGAETPTLA
PLTTQGNLPF RRLCVELGCQ ATYSEMALGM PLLQGSKPDW TLMRAHRSEI TPPKMNPGAI
PLFDDYNHSR DLKFGAQISG SAHWVVTKAA DVLNRYCPHL RVIDLNCGCP IDKVFKSGAG
SALLDASGKM ERMIRGMNAV SGEIPISAKI RTGVRKDRST ATQIIGKLAF GSREHRERLG
APGCAALTLH GRSREQRYTK TADWGYIGEC AALIKTYNDE KAKITDTIAE PDESTLANSK
DGRMYFLGNG DCFSHVDYYE HLEKARVDTV MIGRGALIKP WIFEEIEKGQ YLDKSSTERL
GYIEKFVKYG LEAWGSDELG IGYTRRFLLE YLSFAHRYVP IGLLEHLPPR LNDRPPAYKG
RDEMETLMAS DNYKDWIKIS EMFLGPVHPG FQFQPKHKSN SYEAEG
//
