GenomeNet

Database: UniProt
Entry: A0A151I5V2_9HYME
LinkDB: A0A151I5V2_9HYME
Original site: A0A151I5V2_9HYME 
ID   A0A151I5V2_9HYME        Unreviewed;       652 AA.
AC   A0A151I5V2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00012376};
DE            EC=1.3.1.89 {ECO:0000256|ARBA:ARBA00012376};
GN   ORFNames=ALC53_01130 {ECO:0000313|EMBL:KYM92291.1};
OS   Atta colombica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM92291.1, ECO:0000313|Proteomes:UP000078540};
RN   [1] {ECO:0000313|EMBL:KYM92291.1, ECO:0000313|Proteomes:UP000078540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM92291.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM92291.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Atta colombica WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(47) in tRNA; Xref=Rhea:RHEA:53364, Rhea:RHEA-COMP:13539,
CC         Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC         Evidence={ECO:0000256|ARBA:ARBA00033625};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366;
CC         Evidence={ECO:0000256|ARBA:ARBA00033625};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(47) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(47) in tRNA; Xref=Rhea:RHEA:53360, Rhea:RHEA-COMP:13539,
CC         Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC         Evidence={ECO:0000256|ARBA:ARBA00033656};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362;
CC         Evidence={ECO:0000256|ARBA:ARBA00033656};
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. Dus3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005451}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ976402; KYM92291.1; -; Genomic_DNA.
DR   RefSeq; XP_018055016.1; XM_018199527.1.
DR   RefSeq; XP_018055025.1; XM_018199536.1.
DR   AlphaFoldDB; A0A151I5V2; -.
DR   STRING; 520822.A0A151I5V2; -.
DR   GeneID; 108691664; -.
DR   OrthoDB; 275918at2759; -.
DR   Proteomes; UP000078540; 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; 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; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) 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}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          309..567
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   REGION          72..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  74595 MW;  A4B3D625B0CBC319 CRC64;
     MADYNEKCWD CSFDYGEDKQ KGICLIKEEF IIEDHVRQLS DQCLTKIDKQ KVSTDTDVED
     TSWDQVPAKK AKLEDKREKL RGQNKARPPP FKVSKELSLC PWIADQTTNE SERKCSNQRC
     TFLHDRKKYL KIRPEDIDTE CYIFNLTGKC PRGITCRMGS GHLTEDGFNV IDEKKLEEYS
     KCPPAVKNHL SKDLQNKLRK HKYNFSKAEA IIKANGPSMK KMQLQSLNSK GEDKNTKSDV
     MINISDNSEK VAKHISDNAN VEKMETDASN CNITCKSKEL KIGPVDDSDL IRLRQSEKKT
     IDWNGKILLS PLTTVGNLPF RRICKEYGAD ITCGEMALAP NILKGTQEEW ALVKRHESED
     IFGVQLCGNN PGVLARCAQL LNHEIDADYI DLNLGCPIDM IYKNGGGSGM LNRLNVLETV
     IKSVSQVLDI PLSVKTRTGV YIDKPIAHNL MPRFRDWGVS MITVHGRSRE QRYTKLADWE
     YIEKCAVAAQ PIPVFGNGDI LSFDDYRRTK ETYSTVQGIT IGRGAVIKPW IFTEIKERKL
     IDISSAERFD ILKKYANYGL EHWGSDTRGV ENTRRFMLEW ISFLHRYIPV GILERPPQRI
     NERPPFYRGR DDMETLMASS NCADWVKLSE MLLGKVPDGF RFLPKHKANS WK
//
DBGET integrated database retrieval system