ID   DUSC_AZOVI     STANDARD;      PRT;   309 AA.
AC   P96192;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   tRNA-dihydrouridine synthase C (EC 1.-.-.-).
GN   Name=dusC;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UW;
RX   MEDLINE=97261869; PubMed=9108283; DOI=10.1007/s004380050409;
RA   Manna A.C., Das H.K.;
RT   "Characterization and mutagenesis of the leucine biosynthetic genes of
RT   Azotobacter vinelandii: an analysis of the rarity of amino acid
RT   auxotrophs.";
RL   Mol. Gen. Genet. 254:207-217(1997).
CC   -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified
CC       base found in the D-loop of most tRNAs (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SIMILARITY: Belongs to the dus family. DusC subfamily.
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CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
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DR   EMBL; Y11280; CAA72146.1; -.
DR   InterPro; IPR001269; Du_synth.
DR   Pfam; PF01207; Dus; 1.
DR   PROSITE; PS01136; UPF0034; FALSE_NEG.
KW   FAD; Flavoprotein; Oxidoreductase; tRNA processing.
SQ   SEQUENCE   309 AA;  33181 MW;  2D40B965C6DF551B CRC64;
     MRIALAPMEG LVDELLRDLL TRVGGIDWCV TEFVRVCDRL LPVAQFEKLA PELRHGWRTR
     AGTPMHLQLL GSDPACLAEN AALAAELGAP AIDLNFGCPA KTSTARGADG CCSTSRNCCM
     PSSARCAGPC RRCAGDRQDA PGVRPARGRP GVRRALVEGG VAHLVVHART KVEGYRPPAS
     WEWLARVREA VAVPVYANRK SGRRRIGCRE ISGVEDVMLG CGLVSRPDLA RQIAMRAPDA
     RSSRRAGVRY SRWCASSGGA PGSGSRRATP LAGSSSGWAC WRAVIRRRPR CSPNCAGRTT
     AGGWMPCWA
//