GenomeNet

Database: UniProt
Entry: A0A1E5REK1_9ASCO
LinkDB: A0A1E5REK1_9ASCO
Original site: A0A1E5REK1_9ASCO 
ID   A0A1E5REK1_9ASCO        Unreviewed;       398 AA.
AC   A0A1E5REK1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   SubName: Full=tRNA-dihydrouridine(20) synthase [NAD(P)+] {ECO:0000313|EMBL:OEJ85338.1};
GN   ORFNames=AWRI3579_g1727 {ECO:0000313|EMBL:OEJ85338.1};
OS   Hanseniaspora osmophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ85338.1, ECO:0000313|Proteomes:UP000095728};
RN   [1] {ECO:0000313|Proteomes:UP000095728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(2016).
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   -!- 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:OEJ85338.1}.
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; LPNM01000007; OEJ85338.1; -; Genomic_DNA.
DR   STRING; 56408.A0A1E5REK1; -.
DR   InParanoid; A0A1E5REK1; -.
DR   OrthoDB; 276273at2759; -.
DR   Proteomes; UP000095728; 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   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; PTHR45936; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR   PANTHER; PTHR45936:SF1; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   4: Predicted;
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:UP000095728};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          32..313
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   REGION          347..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  44857 MW;  33BF78E76E7E35B1 CRC64;
     MVTYAGKLCL APMVRAGELP TRLLALRHGA DLVWSPEIID KKLVQCRRVE NDXLQTVDFV
     APCNNSKEFK EQVVFRVFPK EEKGKLIFQM GTSNPGLAVE AALKVINDVS GIDVNAGCPK
     HFSIHSGMGA ALLQTPELLC NILTELVQKV GQPHEKPISV KIRVLDDEPA TLTLVEKLVK
     TGISNLTVHC RTTPMRNRES PIRDYLPSIF EICSKNNVSL VMNGGMKNKK EFLSIRKELG
     LSDSIGGMFA EAAEANPTVF KDEPLQWFEV TKSYLDIARN FDHPYSNVKY MMTRIIPGKE
     KLHKVFSQTK SMQEIDHIIS NWVDPEVGKC ELHSIQKYMG ELRAQEKLAK QEAGKRKQRE
     QQQKDKLANT NKRKQQQQQQ QQENAGADNS PEAKKLKV
//
DBGET integrated database retrieval system