ID A0A1V8SF39_9PEZI Unreviewed; 531 AA.
AC A0A1V8SF39;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00038890};
DE EC=1.3.1.88 {ECO:0000256|ARBA:ARBA00038890};
GN ORFNames=B0A48_16454 {ECO:0000313|EMBL:OQN97590.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN97590.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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(16) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00035900};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382;
CC Evidence={ECO:0000256|ARBA:ARBA00035900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00036049};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378;
CC Evidence={ECO:0000256|ARBA:ARBA00036049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00035864};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374;
CC Evidence={ECO:0000256|ARBA:ARBA00035864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00035813};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370;
CC Evidence={ECO:0000256|ARBA:ARBA00035813};
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. Dus1 subfamily.
CC {ECO:0000256|ARBA:ARBA00038313}.
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:OQN97590.1}.
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DR EMBL; NAJO01000052; OQN97590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SF39; -.
DR STRING; 1507870.A0A1V8SF39; -.
DR InParanoid; A0A1V8SF39; -.
DR OrthoDB; 5487726at2759; -.
DR Proteomes; UP000192596; 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; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 1.
DR PANTHER; PTHR11082:SF5; TRNA-DIHYDROURIDINE(16_17) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
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 mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 21..278
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59371 MW; 722904DFA35C628E CRC64;
MAPRLHGRTF YESIGSPKLV LAPMVDQSEF AWRLLTRSFL PAGLRTSILA YSPMLHAKIF
SQNPKYREDH FRPRKTGAAT EKPEAVGAEA EGESNDWHLD GNPSLDRPLF MQFCANDPAL
FLEAAKHVQP YCDAVDLNLG CPQGIAKKGR YGAFLQEDWD LIYKLINTLH KELDIPVTAK
FRIQETREKT LEYAKMILSA GASIITVHGR RREQKGHNTG LADWEMIKFL RDELPKETVI
FANGNILQHG DIQKCLNATG ADGVMSAEGN LYDPAILAPP PPVGEEGREY WRGKNGLGGY
RMDAVLRRYL DILYIHVLEQ SPPHREPLFL ASDPQSAAVP TPEATPPADG PPAKRQKLDA
EVKRKDKKVT DTNFTAMQAH LFHLLRALIS KHTNVRDALA RSRAGDMPAY ENVLRLVEAA
TKEGLIEYER DPSLYEPESE ADAEVDWQSS DAAVRRCKRP YWVCQSHVRP LPEEAVLKGS
IQLSKKELAR RQREEEESKA AGLQAGGTVE QVATNGVERA EEIPREGMVC G
//
