ID TRMB_CHRSD Reviewed; 246 AA. AC Q1QSR9; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase; DE EC=2.1.1.33; DE AltName: Full=tRNA(m7G46)-methyltransferase; GN Name=trmB; OrderedLocusNames=Csal_3145; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-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; CP000285; ABE60489.1; -; Genomic_DNA. DR RefSeq; YP_575188.1; -. DR GeneID; 4028612; -. DR GenomeReviews; CP000285_GR; Csal_3145. DR KEGG; csa:Csal_3145; -. DR NMPDR; fig|290398.4.peg.3137; -. DR HOGENOM; Q1QSR9; -. DR OMA; Q1QSR9; TKFENRG. DR BioCyc; CSAL290398:CSAL_3145-MON; -. 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 1 246 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000288137. FT REGION 224 227 Substrate binding (Potential). FT BINDING 74 74 S-adenosyl-L-methionine (By similarity). FT BINDING 99 99 S-adenosyl-L-methionine (By similarity). FT BINDING 126 126 S-adenosyl-L-methionine (By similarity). FT BINDING 149 149 S-adenosyl-L-methionine (By similarity). FT BINDING 153 153 Substrate (By similarity). FT BINDING 185 185 Substrate (Potential). SQ SEQUENCE 246 AA; 27368 MW; A691A52734B6E9B4 CRC64; MSDSSSSSEN APATPESPGR PPRGIKSYVL RAGRMTAAQS RGLEEVWPRL GLSVAEGRQS LEALFGRRAP CVVEVGFGMG QSLVEQAAAN PETDFIGIEV HAPGVGKLLD EADKRGLTNL RVYRDDALEV LDKCLPESSL TGLQLFFPDP WPKKKHHKRR IVQPAFVELV RTRLAPHGYL HMATDWEAYA EHMVEVMEEA PGYRNTAPPE SAPYVPRPEF RPLTKFESRG ERLGHGVWDL IYARVE //