(data stored in SCRATCH zone)

SWISSPROT: A5GR56_SYNR3

ID   A5GR56_SYNR3            Unreviewed;       335 AA.
AC   A5GR56;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   Name=dus {ECO:0000313|EMBL:CAK27365.1};
GN   OrderedLocusNames=SynRCC307_0462 {ECO:0000313|EMBL:CAK27365.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27365.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) 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; CT978603; CAK27365.1; -; Genomic_DNA.
DR   RefSeq; WP_011934880.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0462; -.
DR   EnsemblBacteria; CAK27365; CAK27365; SynRCC307_0462.
DR   KEGG; syr:SynRCC307_0462; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217855; -.
DR   OMA; RPWLFAD; -.
DR   OrthoDB; 1710586at2; -.
DR   BioCyc; SSP316278:G1GJL-462-MONOMER; -.
DR   Proteomes; UP000001115; 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; IPR004652; tRNA_dU_NifR3.
DR   InterPro; IPR001269; tRNA_hU_synthase.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   TIGRFAMs; TIGR00737; nifR3_yhdG; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GR56.
DR   SWISS-2DPAGE; A5GR56.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   ACT_SITE    109    109       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006621-1}.
SQ   SEQUENCE   335 AA;  35264 MW;  9362D989237418CB CRC64;
     MPTGSLTLGG HGVTRTLHSR VLQSPLAGVS DKVFRRLVRR WCPDALLFTE MVNATSLELG
     HGRGKVEELA TEEGPIGVQL FDYRPQAMAE AAKRAEGAGA FLIDINMGCP VKKIAKKGGG
     SGLIREPDLA ARIVEAVSQA VQVPVTVKTR LGWCGSDADP VTWCQQLQNA GAQLLTLHGR
     TREQGFKGHA DWQAIAQVKA ALTIPVIANG DINTPDDAQR CLAITGADGV MVGRGSMGAP
     WLVGQIDAAL RGLPMPLAPD ASGRLQLAKE QLLALVSERG DHGLLIARKH MGWTCTGFPG
     APQLRHQLMR APTPDAAVEL LNAAAASIET AAAAG
//

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