ID A1D7K9_NEOFI Unreviewed; 443 AA.
AC A1D7K9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=tRNA dihydrouridine synthase (Smm1), putative {ECO:0000313|EMBL:EAW21703.1};
GN ORFNames=NFIA_068730 {ECO:0000313|EMBL:EAW21703.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21703.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS027690; EAW21703.1; -; Genomic_DNA.
DR RefSeq; XP_001263600.1; XM_001263599.1.
DR AlphaFoldDB; A1D7K9; -.
DR STRING; 331117.A1D7K9; -.
DR EnsemblFungi; EAW21703; EAW21703; NFIA_068730.
DR GeneID; 4590246; -.
DR KEGG; nfi:NFIA_068730; -.
DR VEuPathDB; FungiDB:NFIA_068730; -.
DR eggNOG; KOG2334; Eukaryota.
DR HOGENOM; CLU_013299_3_2_1; -.
DR OMA; GPIRTNS; -.
DR OrthoDB; 276273at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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:UP000006702};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 99..277
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 385..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 47843 MW; F955D30B1B035191 CRC64;
MTSLTTPRVP IPANGVDYRG KVVLAPMVRS GELPSRLLAL KYGADLVWGP ETIDRSLIGA
TRRVNPRNGC IEYIRFPSNG GRPDKPAQES ILYRIDPVRE KGKLVFQIGS ANPELAVEAA
KLVAGDVAGI DLNSGCPKPF STSGGMGAAL LRTPDKLVSI LESLVREVGN PYQIGISVKI
RILETPEKTE SLVKRLVATG ITGLTVHCRT TPMRPRERAI RDQLAMIARI CREAGVACVM
NGDVTSRDEA LALMKEFGVD GAMIATAAEA NPSCFRSEAE GGLLPWREVV HDYLQAAIEC
ENRFGNTKFL LNILIPGKNR EFKDAKTAKS YSDYCHFLKF DDLLPGAAQV DKVLNLTDKS
VYKNNETEDS ARDIAVKNAL ENNETARAAS GAPRPKAASP AVNGGGPIRT SSIPAPVRSK
PEDHPIDINI PAPEMAQKQE LAA
//