(data stored in SCRATCH zone)

SWISSPROT: Q3IG92_PSEHT

ID   Q3IG92_PSEHT            Unreviewed;       310 AA.
AC   Q3IG92;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 85.
DE   RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000256|HAMAP-Rule:MF_02041};
DE            EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02041};
DE            EC=1.3.1.91 {ECO:0000256|HAMAP-Rule:MF_02041};
DE   AltName: Full=U20-specific dihydrouridine synthase {ECO:0000256|HAMAP-Rule:MF_02041};
DE            Short=U20-specific Dus {ECO:0000256|HAMAP-Rule:MF_02041};
DE   AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000256|HAMAP-Rule:MF_02041};
GN   Name=dusA {ECO:0000256|HAMAP-Rule:MF_02041,
GN   ECO:0000313|EMBL:CAI85589.1};
GN   OrderedLocusNames=PSHAa0499 {ECO:0000313|EMBL:CAI85589.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85589.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85589.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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. Specifically modifies
CC       U20 and U20a in tRNAs. {ECO:0000256|HAMAP-Rule:MF_02041}.
CC   -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20) in tRNA + NAD(P)(+) =
CC       uracil(20) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}.
CC   -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20a) in tRNA + NAD(P)(+) =
CC       uracil(20a) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the Dus family. DusA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02041}.
CC   -!- SIMILARITY: Belongs to the dus family.
CC       {ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02041}.
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DR   EMBL; CR954246; CAI85589.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3IG92; -.
DR   STRING; 326442.PSHAa0499; -.
DR   EnsemblBacteria; CAI85589; CAI85589; PSHAa0499.
DR   KEGG; pha:PSHAa0499; -.
DR   PATRIC; fig|326442.8.peg.468; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000259834; -.
DR   KO; K05539; -.
DR   OMA; TFIIHAR; -.
DR   OrthoDB; POG091H068N; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_02041; DusA_subfam; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR004653; DusA.
DR   InterPro; IPR001269; tRNA_hU_synthase.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   PANTHER; PTHR42907:SF2; PTHR42907:SF2; 1.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   TIGRFAMs; TIGR00742; yjbN; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IG92.
DR   SWISS-2DPAGE; Q3IG92.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02041,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02041};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02041,
KW   ECO:0000256|PIRNR:PIRNR006621, ECO:0000313|EMBL:CAI85589.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_02041};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02041,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   NP_BIND     193    195       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   NP_BIND     215    216       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   ACT_SITE     82     82       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02041, ECO:0000256|PIRSR:PIRSR006621-
FT                                1}.
FT   BINDING      52     52       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   BINDING     121    121       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   BINDING     153    153       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   SITE         79     79       Interacts with tRNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_02041}.
FT   SITE        165    165       Interacts with tRNA; defines subfamily-
FT                                specific binding signature.
FT                                {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   SITE        168    168       Interacts with tRNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_02041}.
FT   SITE        281    281       Interacts with tRNA; defines subfamily-
FT                                specific binding signature.
FT                                {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   SITE        284    284       Interacts with tRNA; defines subfamily-
FT                                specific binding signature.
FT                                {ECO:0000256|HAMAP-Rule:MF_02041}.
SQ   SEQUENCE   310 AA;  34884 MW;  FA360D3053162843 CRC64;
     MLDWTDRHCR TFHRKMTKHT VLYTEMITTG AILFGRGDYL HFNQHEGPVA LQLGGSDPQA
     LAQCAKLAGE RGYDEINLNV GCPSDRVQNG RFGACLMGEP QLVADCVAAM KAEVNIPVTV
     KTRIGIDEQD SYEFLCALIE ASHNVGCDDF IIHARKAWLK GLSPKENREV PPLDYPRVYQ
     LKKDYPQLDL SLNGGVKTIE QSLEHLQHID GVMIGREAYS NPFILNEVDE KIYGDIANTQ
     SRHDVVRSMY SYIEDEMRLG ANFWHVARHM LGIFQGQPGA RGFRRHLSEN GHGKQADLSV
     MDKALSFVPE
//

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