ID A0A093ZB05_9PEZI Unreviewed; 349 AA.
AC A0A093ZB05;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DUS-like FMN-binding domain-containing protein {ECO:0000259|Pfam:PF01207};
GN ORFNames=V492_04042 {ECO:0000313|EMBL:KFY12173.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY12173.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY12173.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY12173.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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=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:KFY12173.1}.
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DR EMBL; JPJU01001314; KFY12173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ZB05; -.
DR STRING; 1420902.A0A093ZB05; -.
DR HOGENOM; CLU_013299_4_0_1; -.
DR Proteomes; UP000029299; 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:SF31; TRNA-DIHYDROURIDINE(20A_20B) 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:UP000029299};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 41..304
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
SQ SEQUENCE 349 AA; 37937 MW; DDD23CDF941272AB CRC64;
MAGNYVGGSD VKDGLPPLDH VNPMKLFDIA KEQGRPLYTS APMVRYSKLA FRQTVHKYGV
DLCWTPMILA KEFNRSIFAR DSDFTLPESP TSVPTILQFG ANSPLEFARA TSTMAPFVSG
VDLNCGCPQS WACAECLGAA LMNKRELVAD IVKEAKATLK RDGYEGRRTV SVKIRIHKDL
RQTMDFIKTV QDAGVDFLTI HGRTKAQRSS EPVNTAALST LRSHVTVPLI ANGDVSTLAI
ANSIAAETGV DGVMSARDLL ANPALFAGYD VCPWVAVEQF VNRVVRAPIP FKLVVHHLSQ
MTGSAGGGKP ALLGKEERAE LMECRDMIDV IDFLDRVKGI TRLCKGAGL
//
