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Database: UniProt
Entry: A0A166XYR0_9PEZI
LinkDB: A0A166XYR0_9PEZI
Original site: A0A166XYR0_9PEZI 
ID   A0A166XYR0_9PEZI        Unreviewed;       597 AA.
AC   A0A166XYR0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00038890};
DE            EC=1.3.1.88 {ECO:0000256|ARBA:ARBA00038890};
DE   Flags: Fragment;
GN   ORFNames=CT0861_10240 {ECO:0000313|EMBL:KZL77093.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL77093.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL77093.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL77093.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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:KZL77093.1}.
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DR   EMBL; LFIV01000010; KZL77093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166XYR0; -.
DR   STRING; 708197.A0A166XYR0; -.
DR   OrthoDB; 5487726at2759; -.
DR   Proteomes; UP000076552; 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:UP000076552};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          102..325
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   REGION          313..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL77093.1"
SQ   SEQUENCE   597 AA;  65865 MW;  1EA6FAC36A17CE07 CRC64;
     LEGVFRLWRL RTSQTSRLAR FFSSTKMATT TEAPTAGLET GAAATPKPKL HGRAFYESIG
     SPKYILAPMV DQSEFSANVS DDGLQAWRML SRSFIPPSEQ KNLVAYTPMF HARLYKDTEN
     YRQCHFQAVR PSDSNDPNST PQAWLDGNPS IDRPLFVQFC ANDPDALLGA ALRVAPYCDA
     VDLNLGCPQG IAKKGKYGAF LQEDQELIFK LINTLHQNLP IPVTAKIRIL DTKEATLAYA
     KNVLSAGASI LTVHGRLREQ KGHLTGLADW SIIKWLREQL PPETVLFANG NILQHDDLQR
     ALEATGADGI MSAEGNLSDP TIFSRPPEPG TETREYWRGK DGRGGYRVDA VMRRYMDILH
     KYAAGEKPPS RRPLFVPGDD TAWMEEMDKA LAEEDEPERK KRRKDTPKLG KSRMLSPNYS
     AMQPHMFHLL RHFVSKHTDV RDLLAKSRAG DLEAYEKILS MVERKVADGL IEYEKVGAAM
     FEGDEVLGPA ADAEEVIEED GESSRGAIKR CKRAWWVVQP IIRPLPKEAM AKGAVSLSKK
     DKAKLGKAGD GEVANGEAAV AAPAAAEAVN GKAEGEKTAG QSVQEKVLET DDKLLAG
//
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