ID TRMB_BURCM Reviewed; 255 AA. AC Q0BHL9; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase; DE EC=2.1.1.33; DE AltName: Full=tRNA(m7G46)-methyltransferase; GN Name=trmB; OrderedLocusNames=Bamb_0795; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; 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., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at CC position 46 (m7G46) in tRNA (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L- CC homocysteine + tRNA containing N(7)-methylguanine. CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmB CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000440; ABI86354.1; -; Genomic_DNA. DR RefSeq; YP_772688.1; -. DR GeneID; 4308978; -. DR GenomeReviews; CP000440_GR; Bamb_0795. DR KEGG; bam:Bamb_0795; -. DR NMPDR; fig|339670.3.peg.3019; -. DR OMA; Q0BHL9; TKFENRG. DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:HAMAP. DR HAMAP; MF_01057; -; 1. DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase. DR PANTHER; PTHR23417:SF1; Methyltransf_4; 1. DR Pfam; PF02390; Methyltransf_4; 1. DR TIGRFAMs; TIGR00091; CHP91; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1 255 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000288129. FT REGION 232 235 Substrate binding (Potential). FT BINDING 86 86 S-adenosyl-L-methionine (By similarity). FT BINDING 111 111 S-adenosyl-L-methionine (By similarity). FT BINDING 138 138 S-adenosyl-L-methionine (By similarity). FT BINDING 161 161 S-adenosyl-L-methionine (By similarity). FT BINDING 165 165 Substrate (By similarity). FT BINDING 197 197 Substrate (Potential). SQ SEQUENCE 255 AA; 28399 MW; C98B681217D2EFE7 CRC64; MMHDDPNEAG LPPDDAALPD EAADGADEVN PLHHRRIRSF VTRAGRVSTG QRRALDEFGP RFVVPYAAEI PDWDAVFGRS APRILEIGFG MGASTAEIAA HRPGDDFLGV EVHEPGVGAL LKLIGEQDLP NIRIIQHDAV EVLEHMLAPE SLDGVHIFFP DPWHKARHHK RRLIQPPLVA HLASRLKPGA YLHCATDWQN YAEQMLEVLG AEPSLENTAA DYAPRPDYRP ITKFERRGLR LGHGVWDLVF RKRAG //