ID TRMB_BUCAP Reviewed; 239 AA. AC Q8K927; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 41. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase; DE EC=2.1.1.33; DE AltName: Full=tRNA(m7G46)-methyltransferase; GN Name=trmB; OrderedLocusNames=BUsg_533; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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 -!- SUBUNIT: Monomer (By similarity). 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; AE013218; AAM68074.1; -; Genomic_DNA. DR RefSeq; NP_660863.1; -. DR GeneID; 1005542; -. DR GenomeReviews; AE013218_GR; BUsg_533. DR KEGG; bas:BUsg533; -. DR HOGENOM; Q8K927; -. DR OMA; Q8K927; HELEGYH. DR BioCyc; BAPH198804:BUSG533-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 1 239 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000171308. FT REGION 217 220 Substrate binding (Potential). FT BINDING 69 69 S-adenosyl-L-methionine (By similarity). FT BINDING 94 94 S-adenosyl-L-methionine (By similarity). FT BINDING 121 121 S-adenosyl-L-methionine (By similarity). FT BINDING 144 144 S-adenosyl-L-methionine (By similarity). FT BINDING 148 148 Substrate (By similarity). FT BINDING 180 180 Substrate (Potential). SQ SEQUENCE 239 AA; 27959 MW; 7F8ABFEA7E9A682B CRC64; MKNNIITPQY NCNGTFLRKN RSFVCRKGRI TKSQLQAIEK YWLSIGIDFK LEPLDFTSVF KNSAPVILEI GFGSGESLVK TAANFPNKNF LGIEVYKSGI GSCLRLAHYS GINNLKIIYH DAIEVIDQMI LDHTLSKVQI FFPDPWNKKR HHKRRMIQDF FLIKILKKLN NDGILHIVTD SKEYNFFILN LIQNIDNYIN LSKKRMCFEH FKYRLVTNFE KKAKLSGNKI FDLIFKLKK //