(data stored in SCRATCH zone)

SWISSPROT: Q3IIC1_PSEHT

ID   Q3IIC1_PSEHT            Unreviewed;       326 AA.
AC   Q3IIC1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 84.
DE   RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000256|HAMAP-Rule:MF_02042};
DE            EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02042};
GN   Name=dusB {ECO:0000256|HAMAP-Rule:MF_02042,
GN   ECO:0000313|EMBL:CAI85445.1};
GN   OrderedLocusNames=PSHAa0347 {ECO:0000313|EMBL:CAI85445.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85445.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85445.1, 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. {ECO:0000256|HAMAP-
CC       Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil in tRNA + NAD(P)(+) = uracil
CC       in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02042}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the Dus family. DusB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02042}.
CC   -!- SIMILARITY: Belongs to the dus family.
CC       {ECO:0000256|PIRNR:PIRNR006621}.
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DR   EMBL; CR954246; CAI85445.1; -; Genomic_DNA.
DR   RefSeq; WP_011327059.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIC1; -.
DR   STRING; 326442.PSHAa0347; -.
DR   EnsemblBacteria; CAI85445; CAI85445; PSHAa0347.
DR   KEGG; pha:PSHAa0347; -.
DR   PATRIC; fig|326442.8.peg.330; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217855; -.
DR   KO; K05540; -.
DR   OMA; RHYTNYF; -.
DR   OrthoDB; POG091H02GM; -.
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:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-HAMAP.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 1.10.1200.80; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_02042; DusB_subfam; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR032887; DusB.
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   PANTHER; PTHR11082; PTHR11082; 1.
DR   PANTHER; PTHR11082:SF35; PTHR11082:SF35; 1.
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; Q3IIC1.
DR   SWISS-2DPAGE; Q3IIC1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02042,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02042};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02042,
KW   ECO:0000256|PIRNR:PIRNR006621, ECO:0000313|EMBL:CAI85445.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_02042};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02042,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   NP_BIND      19     21       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   NP_BIND     203    205       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   NP_BIND     227    228       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   ACT_SITE    103    103       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02042, ECO:0000256|PIRSR:PIRSR006621-
FT                                1}.
FT   BINDING      73     73       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   BINDING     142    142       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
SQ   SEQUENCE   326 AA;  36232 MW;  B219D33C268CD431 CRC64;
     MNIVRIGKYQ LENNVIVAPM AGVTDRPFRQ LCRRLGAGLA VSEMLSSNPD VWKTEKSMNR
     MDHSGESGIR AVQIAGADPE LMAQAAQFNV ANGAQIIDIN MGCPAKKVNK KLAGSALLQF
     PELVEEIIDA VVNAVDIPVT LKIRTGWDLD NRNGVEIARI AERYGIASLA VHGRTRACMY
     KGEAEYATIR DIKRSVSIPV VANGDITSPE KAKQVLDYTG ADAIMIGRAA QGRPWIFREI
     DHYLRTGEHL QPPAIAEVRS ILMEHLTNLH TFYGEPMGAR IARKHVSWYL QTHDRDGQFR
     RVFNTIDNPL TQVDVLEQYF KTLAAN
//

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