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Database: UniProt
Entry: V5D2B4_TRYCR
LinkDB: V5D2B4_TRYCR
Original site: V5D2B4_TRYCR 
ID   V5D2B4_TRYCR            Unreviewed;       554 AA.
AC   V5D2B4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=TCDM_10821 {ECO:0000313|EMBL:ESS61581.1};
OS   Trypanosoma cruzi Dm28c.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS61581.1, ECO:0000313|Proteomes:UP000017861};
RN   [1] {ECO:0000313|EMBL:ESS61581.1, ECO:0000313|Proteomes:UP000017861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dm28c {ECO:0000313|EMBL:ESS61581.1,
RC   ECO:0000313|Proteomes:UP000017861};
RX   PubMed=24482508;
RA   Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA   Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT   "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL   Genome Announc. 2:e01114-13(2014).
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   -!- 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:ESS61581.1}.
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DR   EMBL; AYLP01000268; ESS61581.1; -; Genomic_DNA.
DR   EnsemblProtists; ESS61581; ESS61581; TCDM_10821.
DR   VEuPathDB; TriTrypDB:TCDM_10821; -.
DR   Proteomes; UP000017861; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017861};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          100..384
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   REGION          63..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  61841 MW;  AF0552FE5AF826F3 CRC64;
     MAYNETLLEK YRGLVRRGEP FRSSTCPYCN GPRSAGIKHI DPKRKPQSPW DFWDNIVCAP
     TAARSNDGSD AHDHVENEGV ALGAEQTHRA PPRRRPMYVV GPMVDQSELP FRMLCRRYGA
     TLAYSPMLHA RSFAQSAQYR ARYFSTTPHR AEPAMTATAS GEGEAAEDAG RTSDGEETDH
     PLFVQFCGND ADTLLAAARH VEDDCEAVDV NLGCPQGIAR RGYYGSFLME DWDRVHNILH
     CLAVELRVPV TAKMRVFDDD ALTXXXLKYA EMLRDTGIAV LCVHGRTRHN KRGLADMEKI
     RRVREHLRGS IPVIGNGNVL TFEDVRRNMS ATMTDGYMCA EPLLWDPRLF AAPLHPVRNG
     RCFAECREAR LDAIRTAQEY LQLVQRYPVD LAFVKAHLFK MLFHSYEMHP VMHRWLTNFS
     CNGRGGNNNN NAGSEVNGEV EDGDIDDGRS PDGASKSGSG NANKAESNMK QAAGNLDFFA
     FAMDALGEHL RRLYAAEVSC GVEGPQPKRA QEREKGVIED TSXXXXSAER KVETSHDAFA
     EDDVFGIDFD LNKK
//
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