(data stored in ACNUC8465 zone)

SWISSPROT: DUS3_CANGA

ID   DUS3_CANGA              Reviewed;         640 AA.
AC   Q6FJ14;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 87.
DE   RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)];
DE            EC=1.3.1.89;
DE   AltName: Full=tRNA-dihydrouridine synthase 3;
GN   Name=DUS3; OrderedLocusNames=CAGL0M09977g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified
CC       base found in the D-loop of most tRNAs. Specifically modifies U47
CC       in cytoplasmic tRNAs (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(47) in tRNA + NAD(P)(+) =
CC       uracil(47) in tRNA + NAD(P)H.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily.
CC       {ECO:0000305}.
DR   EMBL; CR380959; CAG62758.1; -; Genomic_DNA.
DR   RefSeq; XP_449780.1; XM_449780.1.
DR   ProteinModelPortal; Q6FJ14; -.
DR   SMR; Q6FJ14; -.
DR   STRING; 284593.XP_449780.1; -.
DR   PRIDE; Q6FJ14; -.
DR   EnsemblFungi; CAG62758; CAG62758; CAGL0M09977g.
DR   KEGG; cgr:CAGL0M09977g; -.
DR   CGD; CAL0136961; CAGL0M09977g.
DR   EuPathDB; FungiDB:CAGL0M09977g; -.
DR   eggNOG; KOG2333; Eukaryota.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000240610; -.
DR   InParanoid; Q6FJ14; -.
DR   KO; K05544; -.
DR   OMA; WALMKAH; -.
DR   OrthoDB; EOG092C20WI; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102265; F:tRNA-dihydrouridine47 synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 4.10.1000.10; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR001269; tRNA_hU_synthase.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR11082; PTHR11082; 1.
DR   Pfam; PF01207; Dus; 2.
DR   PROSITE; PS01136; UPF0034; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJ14.
DR   SWISS-2DPAGE; Q6FJ14.
KW   Complete proteome; Cytoplasm; Flavoprotein; FMN; Metal-binding; NAD;
KW   NADP; Nucleus; Oxidoreductase; Reference proteome; Repeat;
KW   tRNA processing; Zinc; Zinc-finger.
FT   CHAIN         1    640       tRNA-dihydrouridine(47) synthase
FT                                [NAD(P)(+)].
FT                                /FTId=PRO_0000330233.
FT   ZN_FING      70    104       C3H1-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00723}.
FT   ZN_FING     116    146       C3H1-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00723}.
FT   NP_BIND     273    275       FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
FT   NP_BIND     486    488       FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
FT   NP_BIND     510    511       FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
FT   ACT_SITE    361    361       Proton donor.
FT                                {ECO:0000250|UniProtKB:Q5SMC7}.
FT   BINDING     328    328       FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
FT   BINDING     401    401       FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
FT   BINDING     432    432       FMN. {ECO:0000250|UniProtKB:Q5SMC7}.
SQ   SEQUENCE   640 AA;  73628 MW;  157B2917D5F77A56 CRC64;
     MKRELEGSYE SERKRGVAQV KAEYVVGAAS NVRVDEEEAG SERFVQGEFG GKKNKKKRGQ
     NKNRDNRQQK ETHALCPKYV LADVTNQVDL CTFGDNCRFV HDIPTYLEHK RPEITDSVFK
     TCPVFETLGY CPMGFKCRFL SSHMDKETHK LLGEYPSDLA SASHEINHIT QDQKYDLIKK
     RFPFSKSELV LEILDSFQEE NREMHREAEK VKEDQQDNED EQKEKAPQVV QRELEAQKRR
     QRQKDLYLQY KDTRFFAQEK KPLDLRHKKI VSPLTTVGNL PYRRLMRTLG ADVTYSEMAL
     AVPLVQGTNS EWALPKAHES EYPGFGVQVA CSKGWQASKA AEALATYIPN GISEINLNSG
     CPIDLLYRQG SGSALLDNPA RMIRCLNAMN YVSGDIPITV KIRTGTKEGH PIADTLVRRL
     VFETDVAAIT LHGRSRQQRY TKVADWDYVS QVAKALRQAE ADFMESPQGK ESHHDEKTRH
     TQFVGNGDIF NYTDWYQHLE DPEVDSCMVA RGALIKPWIF EEINAQQHLD KTSSERLEIL
     KTYSKFAMDH WGTDEYGIAL GRRFFCEFMS FFHRYIPVGI LERVPVQLNE RPPLWKGRDD
     METLLGSSDV KDWIKLSEMF FGPTEDSFVF TPKHKSSSYK
//

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