ID A0A0G4IZM8_PLABS Unreviewed; 346 AA.
AC A0A0G4IZM8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=PBRA_001809 {ECO:0000313|EMBL:CEP00755.1}, PLBR_LOCUS978
GN {ECO:0000313|EMBL:SPQ93763.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OG Mitochondrion {ECO:0000313|EMBL:SPQ93763.1}.
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEP00755.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEP00755.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEP00755.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPQ93763.1, ECO:0000313|Proteomes:UP000290189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Fogelqvist J.;
RL Submitted (MAR-2018) 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. {ECO:0000256|PIRNR:PIRNR006621}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CDSF01000101; CEP00755.1; -; Genomic_DNA.
DR EMBL; OVEO01000002; SPQ93763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IZM8; -.
DR STRING; 37360.A0A0G4IZM8; -.
DR EnsemblProtists; CEP00755; CEP00755; PBRA_001809.
DR OMA; NNMIGAC; -.
DR OrthoDB; 103046at2759; -.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR Proteomes; UP000290189; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; IPR001269; DUS_fam.
DR InterPro; IPR004653; DusA.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR42907; FMN-LINKED OXIDOREDUCTASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR42907:SF1; FMN-LINKED OXIDOREDUCTASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; 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 ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR006621};
KW Mitochondrion {ECO:0000313|EMBL:SPQ93763.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW Reference proteome {ECO:0000313|Proteomes:UP000039324};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 7..315
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 346 AA; 38780 MW; B61FA54D52200FD1 CRC64;
MTLPVHVAPM MKVTTAPFRH LCRLLNPDAV LYTEMIGARA LVEADSAGRA RLLRRTPDDD
PVVVQLGGSD PDLLCRAAQH CQETGRFPEI NLNLGCPSVA VQSGRFGAAM MLDDNVADTV
KTVASCVDVP ISIKCRIGVD QFDSYDFIHS FVDRVHSRAR VQRFVVHART ALLNRTPKDN
RSIPPLRYDV VHRLKRDFPD LQIVINGGLH LTDDHVIAHA NANMDGVMIG RSVRDDPYQL
RRWRRTSNQH ASDDVEGRVR VVLDYVEFVD MELKSSATRR GGIVPLIMPL LNLFSGTVGS
GTWKRALSAT RSAVPVPDRI RRALDELERA RQGHRERERS MAFLEQ
//
