(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHN2_GEOS0

ID   A0A0F6BHN2_GEOS0        Unreviewed;       333 AA.
AC   A0A0F6BHN2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   OrderedLocusNames=GY4MC1_0077 {ECO:0000313|EMBL:ADP72933.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72933.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72933.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72933.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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; CP002293; ADP72933.1; -; Genomic_DNA.
DR   RefSeq; WP_013399821.1; NC_014650.1.
DR   EnsemblBacteria; ADP72933; ADP72933; GY4MC1_0077.
DR   GeneID; 29237301; -.
DR   KEGG; gmc:GY4MC1_0077; -.
DR   OMA; RPWLFAD; -.
DR   OrthoDB; 1710586at2; -.
DR   BioCyc; GSP581103:G1GOQ-90-MONOMER; -.
DR   Proteomes; UP000002034; 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; A0A0F6BHN2.
DR   SWISS-2DPAGE; A0A0F6BHN2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   ACT_SITE    102    102       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006621-1}.
SQ   SEQUENCE   333 AA;  37023 MW;  BEC32AC0DE833DF5 CRC64;
     MFKIGDVEIK NRVVLAPMAG VCNSAFRLTV KEFGAGLVCA EMVSDKGIVY NNEKTLNMLY
     IDEREKPLSL QIFGGEKETL VEAAKFVDKH TNADIIDINM GCPVPKVTKC DAGAKWLLDP
     NKIYDVVAAI VDAVEKPVTV KMRIGWDENH IYAVENAQAV ERAGGKAVAV HGRTRVQMYE
     GKADWNIIKQ VKEAVNIPVI GNGDVKTPQD AKRMLEETGV DGVMIGRAAL GNPWMIYRTV
     RYLETGELIP EPTVREKIEV CLLHLDRLIA LKGEHIAVKE MRKHAAWYLK GVRGNAKIRN
     AINECETREQ LAALLLNFAE EVESKEQMNA QAV
//

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