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Database: UniProt
Entry: A1D7K9_NEOFI
LinkDB: A1D7K9_NEOFI
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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
//
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