(data stored in SCRATCH zone)

SWISSPROT: D6XY33_BACIE

ID   D6XY33_BACIE            Unreviewed;       343 AA.
AC   D6XY33;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   OrderedLocusNames=Bsel_0570 {ECO:0000313|EMBL:ADH98106.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98106.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98106.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a
CC       modified base found in the D-loop of most tRNAs, via the reduction
CC       of the C5-C6 double bond in target uridines.
CC       {ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the dus family.
CC       {ECO:0000256|PIRNR:PIRNR006621}.
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DR   EMBL; CP001791; ADH98106.1; -; Genomic_DNA.
DR   RefSeq; WP_013171535.1; NC_014219.1.
DR   STRING; 439292.Bsel_0570; -.
DR   EnsemblBacteria; ADH98106; ADH98106; Bsel_0570.
DR   KEGG; bse:Bsel_0570; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217857; -.
DR   OMA; TFIIHAR; -.
DR   OrthoDB; 1710586at2; -.
DR   BioCyc; BSEL439292:G1GLR-613-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
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; -; 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   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XY33.
DR   SWISS-2DPAGE; D6XY33.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   ACT_SITE    105    105       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006621-1}.
SQ   SEQUENCE   343 AA;  38836 MW;  CBE42D1FD9B3F435 CRC64;
     MKENFWHDLP KPFFILAPME AVTDVVFRHV VSEAAAPDVF FTEFANSDSF CHPKGRESLK
     GRLMFTEDEQ PIVAHIWGDK PEHFRTMSVA MAEMGYKGID INMGCPVHNV AGDGKGAGLI
     KRPDVAAELI EAAKAGGLPV SVKTRIGFSK IDEWQNWLRH ILEQDIVNLS IHLRTKKEMS
     DVPAHWELIP DIKALRDEVA PNTLLTINGD IDDRQTGLEL AEKYGVDGIM IGRGIFKNPF
     AFETEPKEHT SEELLGLLRL QLDLHDKYSK DLENRPFTPL QRFFKIYVRS FPKAGELRKK
     LMETKTTDEV RAILDTFEKE KQAEEKAEAE ALCQTASTDH VHS
//

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