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Database: UniProt
Entry: A0A024G769_9STRA
LinkDB: A0A024G769_9STRA
Original site: A0A024G769_9STRA 
ID   A0A024G769_9STRA        Unreviewed;       839 AA.
AC   A0A024G769;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=BN9_029550 {ECO:0000313|EMBL:CCI42171.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI42171.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI42171.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI42171.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI42171.1}.
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DR   EMBL; CAIX01000030; CCI42171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024G769; -.
DR   STRING; 65357.A0A024G769; -.
DR   InParanoid; A0A024G769; -.
DR   OrthoDB; 5487726at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
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; 1.10.340.70; -; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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; PF00385; Chromo; 1.
DR   Pfam; PF01207; Dus; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS50013; CHROMO_2; 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:UP000053237};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          806..839
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
SQ   SEQUENCE   839 AA;  95238 MW;  635A105974B87BE1 CRC64;
     MQKLRGHEFF RSIGSPQRIV APMVDQSELA FRMLCREHGA QLCYTPMFHS RLFAESQEYR
     SRMFEQHVRD RPLIVQFCGN DPETMVTAAK YVEGHCDAVD INLGCPQGIA RKGNYGAFLM
     KDKARVCGIV EKLVDEVAVP VTCKIRVFPD EAETIEFTKM LEKAGCDLLV VHGRTKEMNK
     GTVGQVNWEI IKKIKNALSI PVIANGGIET PEDIAECLEV TGADGVMSSE AILGNPALFD
     KSLQFGPLHQ KGPCYFDLAN EYMDFVTTYP TGNLKIVRAH LFKLLFEDLT HHTDLRSALA
     SANTFSEMKH LLQVLGDRKN APVKYEYTLE NIQFLSNAQG DIPVVRRTSG IGGNAWCVVT
     PMRVLFDKFD FVVVYLDDIC IFSKTNEEDT THLHELFEVL RHEKPYTHRR KCSFGKESVG
     FLGHNVSRNG LSVDKRKTSA IDTMAPPATR KELLSFLGLA GYNRRFICDF AKIALPLSEF
     VKKEVSWEWS DDQDEAFRRL KFTFMLHHVQ GTSNVVADAR SRPSVTGPTI VTRHSQVPQV
     HDCGPVCASR DVHFRRHARH MAVLCLLPRI DQDLLLDMRD FSSVDSVHQV GVLQLQQRES
     HDQIQNIDFI ISSIHLSSIT KKAFMSGYTK DREFKETLNS HHDKYVLPHG LHNVKTNHAA
     KRLCVPADDR LIIAILCEHH DGNTAAHPGV RRTKLKVAQW YYWPTLEKKF ESMYKAATPQ
     VTAPRNGTQT TKTKLLAKEI GPFQIKKMIN NNVAKLALPR NLGKLHPSLN IELLSHFVPN
     PVRFSSRPVP KAVPVIFEKK TGSELYIVEA LVQKRVYKKQ PEWLVEWHGL PEHECTWEK
//
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