ID   TRMFO_JANSC             Reviewed;         458 AA.
AC   Q28PE7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=Jann_2498;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E.,
RA   Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A.,
RA   Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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 + tRNA
CC       containing uridine at position 54 + FADH(2) = tetrahydrofolate +
CC       tRNA containing ribothymidine at position 54 + 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; CP000264; ABD55415.1; -; Genomic_DNA.
DR   RefSeq; YP_510440.1; -.
DR   GeneID; 3934957; -.
DR   GenomeReviews; CP000264_GR; Jann_2498.
DR   KEGG; jan:Jann_2498; -.
DR   HOGENOM; Q28PE7; -.
DR   OMA; Q28PE7; MKPVGLT.
DR   BioCyc; JSP290400:JANN_2498-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:HAMAP.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-...; IEA:EC.
DR   GO; GO:0009021; F:tRNA (uracil-5-)-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:HAMAP.
DR   HAMAP; MF_01037; -; 1.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004417; Gid.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11806; GIDA; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   ProDom; PD003738; GIDA; 1.
DR   TIGRFAMs; TIGR00137; gid_trmFO; 1.
DR   PROSITE; PS01280; GIDA_1; FALSE_NEG.
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    458       Methylenetetrahydrofolate--tRNA-(uracil-
FT                                5-)-methyltransferase trmFO.
FT                                /FTId=PRO_0000346345.
FT   NP_BIND      11     16       FAD (By similarity).
SQ   SEQUENCE   458 AA;  49479 MW;  C5BC5B0F50820C58 CRC64;
     MTQNTQLTII GGGMAGSEAA WQAANLGVNV RLIEMRPKVE TFAHRTGNLA EMVCSNSFRS
     DDSEQNAVGL LHWEMRAANS VIMHTADSHK LPAGGALAVD RDPFAEAVTA KLHAHPNIEI
     TYGEVTDLPA AGPTIIATGP LTGSALADAI AREAGQDALA FFDAIAPIVY ADSIDMDIAW
     RQSRYDKGDT LEEQQAYINC PLTRDQYEAF IDALLSADKT QFKDGETAGY FDGCLPIEVM
     AERGRETLRF GPMKPVGLTN PHDPQTKAYA VVQLRRDNAL GTLYNIVGFQ TKMTYGAQKQ
     VFAMIPGLQE ASFARLGGIH RNTFINSPTL LDDQMRLRSK PHIRFAGQIT GVEGYVESAS
     MGLLAGRMAA AEILGETLPD LPDTTAMGAL VTHITGGADA KTFQPMNVNF GLFPPVEGLK
     GGRRGRKDRY KAYTDRAKAA WTNWLTPQTS LGGSQAAE
//