ID   RIMN_ECOUT              Reviewed;         190 AA.
AC   Q1R650;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   03-APR-2013, entry version 42.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein RimN;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein RimN;
GN   Name=rimN; OrderedLocusNames=UTI89_C3727;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group
CC       on adenosine at position 37 (t(6)A37) in tRNAs that read codons
CC       beginning with adenine (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the SUA5 family. RimN subfamily.
CC   -!- SIMILARITY: Contains 1 YrdC-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE09164.1; Type=Erroneous initiation;
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DR   EMBL; CP000243; ABE09164.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_542695.1; NC_007946.1.
DR   ProteinModelPortal; Q1R650; -.
DR   SMR; Q1R650; 3-188.
DR   STRING; 364106.UTI89_C3727; -.
DR   EnsemblBacteria; ABE09164; ABE09164; UTI89_C3727.
DR   GeneID; 3990039; -.
DR   GenomeReviews; CP000243_GR; UTI89_C3727.
DR   KEGG; eci:UTI89_C3727; -.
DR   PATRIC; 18456926; VBIEscCol42261_3670.
DR   eggNOG; COG0009; -.
DR   HOGENOM; HOG000076163; -.
DR   KO; K07566; -.
DR   OMA; FGLGCNP; -.
DR   ProtClustDB; PRK10634; -.
DR   BioCyc; ECOL364106:GHPQ-3735-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR   GO; GO:0070526; P:threonylcarbamoyladenosine biosynthetic process; IEA:HAMAP.
DR   Gene3D; 3.90.870.10; -; 1.
DR   HAMAP; MF_01852; RimN; 1; -.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR023535; tRNA-t6A_RimN_(YrdC).
DR   InterPro; IPR006070; YrdC-like_dom.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; DHBP_synth_RibB-like_a/b_dom; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding;
KW   RNA-binding; tRNA processing; tRNA-binding.
FT   CHAIN         1    190       tRNA threonylcarbamoyladenosine
FT                                biosynthesis protein RimN.
FT                                /FTId=PRO_0000352915.
FT   DOMAIN        7    190       YrdC-like.
SQ   SEQUENCE   190 AA;  20641 MW;  83AE702A6268E3D1 CRC64;
     MNNNLQGDAI AAAIDVLNEE RVIAYPTEAV FGVGCDPDSE TAVMRLLELK QRPVDKGLIL
     IAANYEQLKP YIDDTMLTDA QRETIFSRWP GPVTFVFPAP ATTPRWLTGR FDSLAVRVTD
     HPLVVALCQA YGKPLVSTSA NLSGLPPCRT VDEVRAQFGA AFPVVPGETG GRLNPSEIRD
     ALTGELFRQG
//