ID U6G704_9EIME Unreviewed; 340 AA.
AC U6G704;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=EPH_0004120 {ECO:0000313|EMBL:CDI75083.1};
OS Eimeria praecox.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI75083.1};
RN [1] {ECO:0000313|EMBL:CDI75083.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI75083.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI75083.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI75083.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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; HG690708; CDI75083.1; -; Genomic_DNA.
DR AlphaFoldDB; U6G704; -.
DR EnsemblProtists; CDI75083; CDI75083; EPH_0004120.
DR VEuPathDB; ToxoDB:EPH_0004120; -.
DR OrthoDB; 103046at2759; -.
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; 2.
DR PIRSF; PIRSF006621; Dus; 2.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 14..226
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT DOMAIN 252..307
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 340 AA; 37483 MW; D88E7A4E4408F96A CRC64;
MGEGILPSRP LLAVAPMIAV SNTHFRNFMR LITRHSTVYT EMVVDSTILH NTHQLEEYLG
FDEIEHPIVC QLGGSNPETL ADAASWAERV GYDELNLNVG CPSCRVVAKG CFGAALMRTP
AKVRDIVHEM KRRVQIPVTV KCRLGVDHLD SPEFTRNFVD TVAQGGCKHF IVHARKAWLQ
GVDPKKNRSV PPLLYERVFE LCDTFPELHF SLNGGVSTLE LADKLLSGEW RKTKDTALAE
PHSGGTGTTE GLQYSGLHGV MIGRAAMNDP CCLAQTDKLI YDTSIRRSAP DETAVEALHH
AMDAVDDEFP GVLDYPLSMG KNPRYEELAS SLGRGVRSSE
//
