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Database: UniProt
Entry: B9QPR1_TOXGV
LinkDB: B9QPR1_TOXGV
Original site: B9QPR1_TOXGV 
ID   B9QPR1_TOXGV            Unreviewed;       653 AA.
AC   B9QPR1; A0A0F7UU00;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Dihydrouridine synthase (Dus) protein {ECO:0000313|EMBL:ESS33365.1};
DE   SubName: Full=Dihydrouridine synthase domain-containing protein {ECO:0000313|EMBL:CEL73531.1};
GN   ORFNames=BN1205_080170 {ECO:0000313|EMBL:CEL73531.1}, TGVEG_280780
GN   {ECO:0000313|EMBL:ESS33365.1};
OS   Toxoplasma gondii (strain ATCC 50861 / VEG).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS33365.1, ECO:0000313|Proteomes:UP000002226};
RN   [1] {ECO:0000313|EMBL:ESS33365.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VEG {ECO:0000313|EMBL:ESS33365.1};
RA   Paulsen I.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA   Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT   "Annotation of Toxoplasma gondii VEG.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ESS33365.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VEG {ECO:0000313|EMBL:ESS33365.1};
RA   Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA   Roos D., Caler E., Lorenzi H.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:CEL73531.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VEG {ECO:0000313|EMBL:CEL73531.1};
RX   PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA   Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA   Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT   "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT   Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT   Transcript Features.";
RL   PLoS ONE 10:e0124473-e0124473(2015).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; LN714496; CEL73531.1; -; Genomic_DNA.
DR   EMBL; AAYL02000106; ESS33365.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9QPR1; -.
DR   STRING; 432359.B9QPR1; -.
DR   PaxDb; 5811-TGME49_080780; -.
DR   EnsemblProtists; ESS33365; ESS33365; TGVEG_280780.
DR   VEuPathDB; ToxoDB:TGVEG_280780; -.
DR   eggNOG; KOG2334; Eukaryota.
DR   OMA; ANTLNYH; -.
DR   Proteomes; UP000002226; Partially assembled 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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          257..497
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  70219 MW;  815EE442BD6700D0 CRC64;
     MPGIAEGEQP LQETARNWDE ACGHGLPRQL DTVEENLNSR KRRKVDGDRM CDADSEGTGL
     APVSSRQTEC VDEKEDGDDS EERKVLGRRP RTTVERPSAL SPSRGSSEDS ASAAPLFSCL
     SPDCAASSLP ASAPAPSSAS ASSSMSETSS PASPPSSSSD SLLSRTHVCA SSDLSLPSRS
     FLSASSSVAA GSVSDALPAR LAPPLSSCPS GSSSCLSSAS STGCRSSASD SVKLLEAEAS
     LHFKPRGLAD RYCGKWILAP MVRIGILPFR LECLKYGADL VYTEETIDHK LLNSVRTFNE
     DFSTIDFLHK SEKTCVFSTC LEERGKVVMQ LGTSDATRAL KAAMLVAQDV AAVDVNMGCP
     KSFSINGGMG AALLKTPLIA TDILKTLRRN LDIPVTCKIR LLDTIHKTID FARLCENCGI
     EAIAIHARET HERPSHRAHW DLFPALKSSL AIPLIANGDF LTRRDADVFQ EKIGADSLMF
     ARGAMWDPSI FSWKKGTTKN VVAEFDSDSS AALSCEKETS SLYTSDPPPM GQNTDFSHPG
     SSLPASESSR VKVMRGYIKR AVVCGAPYQA IKFCLQSMAA QCSSDRNVNL AITSSKSTRD
     LCRALDLDLF YETVFPKLPP HANTLNYHKM RNLPEAASTE RLDSPLAFSS YLS
//
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