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Database: UniProt
Entry: B9DS62
LinkDB: B9DS62
Original site: B9DS62 
ID   TRMFO_STRU0             Reviewed;         444 AA.
AC   B9DS62;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   14-MAY-2014, entry version 41.
DE   RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO;
DE            EC=2.1.1.74;
DE   AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase;
DE   AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase;
GN   Name=trmFO; OrderedLocusNames=SUB0921;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A.,
RA   Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A.,
RA   Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N.,
RA   Whatmore A.M., Bentley S.D., Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
CC   -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-
CC       uridine at position 54 (M-5-U54) in all tRNAs (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + uracil(54) in
CC       tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA +
CC       FAD.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
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DR   EMBL; AM946015; CAR42047.1; -; Genomic_DNA.
DR   RefSeq; YP_002562247.1; NC_012004.1.
DR   ProteinModelPortal; B9DS62; -.
DR   STRING; 218495.SUB0921; -.
DR   PRIDE; B9DS62; -.
DR   EnsemblBacteria; CAR42047; CAR42047; SUB0921.
DR   GeneID; 7391394; -.
DR   KEGG; sub:SUB0921; -.
DR   PATRIC; 19807538; VBIStrUbe20775_0889.
DR   eggNOG; COG1206; -.
DR   HOGENOM; HOG000252054; -.
DR   KO; K04094; -.
DR   OMA; EIYFEGC; -.
DR   OrthoDB; EOG6J74VT; -.
DR   BioCyc; SUBE218495:GJ7D-959-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR   HAMAP; MF_01037; TrmFO; 1.
DR   InterPro; IPR004417; Folate-dep_Ribothymidyl_synth.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR020595; GIDA-rel_CS.
DR   Pfam; PF01134; GIDA; 1.
DR   TIGRFAMs; TIGR00137; gid_trmFO; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN         1    444       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase TrmFO.
FT                                /FTId=PRO_1000149479.
FT   NP_BIND      10     15       FAD (By similarity).
SQ   SEQUENCE   444 AA;  49211 MW;  B66A7FE7F52C9647 CRC64;
     MSQSYINVIG AGLAGSEAAY QIAKRGIPVK LYEMRGVKAT PQHKTSNFAE LVCSNSFRGD
     SLTNAVGLLK EEMRRLDSII MRAGEAHRVP AGGAMAVDRV GYAEAVTAEL ENNPLIEVIR
     GEITEIPNDA ITVIATGPLT SDALAEKIHA LNGGEGFYFY DAAAPIIDKS TINMDKVYLK
     SRYDKGEAAY LNCPMTKEEF LAFHEALTTA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT
     MLYGPMKPVG LEYPDDYKGP RDGDYKTPYA VVQLRQDNAA GSLYNMVGFQ THLKWGEQKR
     VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LKQTFQSRAN ENLFFAGQMT GVEGYVESAA
     SGLVAGINAA RLFKGEEAII FPETTAIGSL PHYVTHTDSK HFQPMNVNFG IIKELEGKRI
     RDKKERYEAI AERSLKDLEA FLNS
//
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