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Database: UniProt
Entry: A0A024G5Y2_9STRA
LinkDB: A0A024G5Y2_9STRA
Original site: A0A024G5Y2_9STRA 
ID   A0A024G5Y2_9STRA        Unreviewed;       817 AA.
AC   A0A024G5Y2;
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_029560 {ECO:0000313|EMBL:CCI42172.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI42172.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI42172.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI42172.1,
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:CCI42172.1}.
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DR   EMBL; CAIX01000030; CCI42172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024G5Y2; -.
DR   STRING; 65357.A0A024G5Y2; -.
DR   InParanoid; A0A024G5Y2; -.
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          784..817
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
SQ   SEQUENCE   817 AA;  92701 MW;  7EF09DEFBA10EEB5 CRC64;
     MVDQSELAFR MLCREHGAQL CYTPMFHSRL FAESQEYRSR MFEQHVRDRP LIVQFCGNDP
     ETMVTAAKYV EGHCDAVDIN LGCPQGIARK GNYGAFLMKD KARVCGIVEK LVDEVAVPVT
     CKIRVFPDEA ETIEFTKMLE KAGCDLLVVH GRTKEMNKGT VGQVNWEIIK KIKNALSIPV
     IANGGIETPE DIAECLEVTG ADGVMSSEAI LGNPALFDKS LQFGPLHQKG PCYFDLANEY
     MDFVTTYPTG NLKIVRAHLF KLLFEDLTHH TDLRSALASA NTFSEMKHLL QVLGDRKNAP
     VKYEYTLENI QFLSNAQGDI PVVRRTSGIG GNAWCVVTPM RVLFDKFDFV VVYLDDICIF
     SKTNEEDTTH LHELFEVLRH EKPYTHRRKC SFGKESVGFL GHNVSRNGLS VDKRKTSAID
     TMAPPATRKE LLSFLGLAGY NRRFICDFAK IALPLSEFVK KEVSWEWSDD QDEAFRRLKF
     TFMLHHVQGT SNVVADARSR PSVTGPTIVT RHSQVPQVHD CGPVCASRDV HFRRHARHMA
     VLCLLPRIDQ DLLLDMRDFS SVDSVHQVGV LQLQQRESHD QIQNIDFIIS SIHLSSITKK
     AFMSGYTKDR EFKETLNSHH DKYVLPHGLH NVKTNHAAKR LCVPADDRLI IAILCEHHDG
     NTAAHPGVRR TKLKVAQWYY WPTLEKKFES MYKAATPQVT APRNGTQTTK TKLLAKEIGP
     FQIKKMINNN VAKLALPRNL GKLHPSLNIE LLSHFVPNPV RFSSRPVPKA VPVIFEKKTG
     SELYIVEALV QKRVYKKQPE WLVEWHGLPE HECTWEK
//
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