(data stored in ACNUC7421 zone)

SWISSPROT: D6ZA62_SEGRD

ID   D6ZA62_SEGRD            Unreviewed;       386 AA.
AC   D6ZA62;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 48.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   OrderedLocusNames=Srot_0113 {ECO:0000313|EMBL:ADG96604.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96604.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96604.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96604.1; -; Genomic_DNA.
DR   RefSeq; WP_013137060.1; NC_014168.1.
DR   STRING; 640132.Srot_0113; -.
DR   EnsemblBacteria; ADG96604; ADG96604; Srot_0113.
DR   KEGG; srt:Srot_0113; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217856; -.
DR   OMA; RPWLFAD; -.
DR   OrthoDB; 1710586at2; -.
DR   BioCyc; SROT640132:G1GLH-115-MONOMER; -.
DR   Proteomes; UP000002247; 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; 1.10.1200.80; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
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; D6ZA62.
DR   SWISS-2DPAGE; D6ZA62.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   ACT_SITE    117    117       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006621-1}.
SQ   SEQUENCE   386 AA;  41501 MW;  C3AEEF0207817989 CRC64;
     MTTTFAAPAL RIGPFELASP VVLAPMAGVT NLAFRTVCRE LETRLTGQAR GLYVNEMVMA
     RSLVNRNPKA MRMIEFGPEE RPRSMQLYTV DPEAVGEAVR MIVAEDLADH VDLNFGCPVP
     KVTRNGGGAA LPYKRRLFAR IIEAAVNGAQ GAVPITVKFR VGIDDEHHTY LDAGRIAQDS
     GAASVALHAR TAAQLYSGTA DWSAIARLKE HVTEIPVLGN GDIFAAADAK RMMDQTGCDG
     VVVGRGCLGR PWLFAELAAA LSGGAIPAPP PPNLGEVARI VLRHAQLLVL HAGSHGVAEM
     RKHFAWYLRG FSVGSELRGK FSTVGSLAEI EDLLGQLPQE EPFPEEAEGP RGRKGSPQKK
     VALPQGWLDD PQDWAVRLDD VEHSGG
//

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