ID TRMB_ARTS2 Reviewed; 319 AA. AC A0K1I7; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 16. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase; DE EC=2.1.1.33; DE AltName: Full=tRNA(m7G46)-methyltransferase; GN Name=trmB; OrderedLocusNames=Arth_3782; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290399; 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., Dalin E., Tice H., RA Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., RA Nakatsu C.H., Richardson P.; RT "Complete sequence of chromosome 1 of Arthrobacter sp. FB24."; 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; CP000454; ABK05157.1; -; Genomic_DNA. DR RefSeq; YP_833257.1; -. DR GeneID; 4447832; -. DR GenomeReviews; CP000454_GR; Arth_3782. DR KEGG; art:Arth_3782; -. DR TIGR; Arth_3782; -. DR OMA; A0K1I7; WVFFPDP. 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 1 319 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000288119. FT REGION 298 301 Substrate binding (Potential). FT BINDING 103 103 S-adenosyl-L-methionine (By similarity). FT BINDING 128 128 S-adenosyl-L-methionine (By similarity). FT BINDING 155 155 S-adenosyl-L-methionine (By similarity). FT BINDING 178 178 S-adenosyl-L-methionine (By similarity). FT BINDING 182 182 Substrate (By similarity). FT BINDING 214 214 Substrate (Potential). SQ SEQUENCE 319 AA; 34907 MW; 66612CE2339DD1A6 CRC64; MSESPETPEP SPAQSPEAAP EQPQAARPVT PGSQASFGTY GGRPVSFVRR GTRLQGRRQQ AWEEHSDRWA VDVPRHIANT SVHPDYVFDA EAEFGRSAPL IVEIGSGLGD AVCHAAEENP DWDFLAVEVY TPGLANTVIK INSRKLSNVR VVEANAPEVL ATMLPAGSVS EVWVFFPDPW HKSRHHKRRL IQPEFAALVA AALKPGGLFR VATDWSNYAV HVRDVMAGSA DFVNLHDGER RGPESPLTQV WQSGVESLVG GAPVKEGRAP VSTEHTGPNE GVDETGGWAP RFEGRIRTSF ENKAHEAGRL IFDLCYRRL //