ID TRMD_BUCAP Reviewed; 262 AA. AC Q8K9F4; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 43. DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase; DE EC=2.1.1.31; DE AltName: Full=M1G-methyltransferase; DE AltName: Full=tRNA [GM37] methyltransferase; GN Name=trmD; OrderedLocusNames=BUsg_383; 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: Specifically methylates guanosine-37 in various tRNAs CC (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L- CC homocysteine + tRNA containing N(1)-methylguanine. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the RNA methyltransferase trmD 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; AAM67935.1; -; Genomic_DNA. DR RefSeq; NP_660724.1; -. DR HSSP; P43912; 1UAJ. DR GeneID; 1005774; -. DR GenomeReviews; AE013218_GR; BUsg_383. DR KEGG; bas:BUsg383; -. DR HOGENOM; Q8K9F4; -. DR OMA; Q8K9F4; HRSVDDT. DR BioCyc; BAPH198804:BUSG383-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IEA:HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:HAMAP. DR HAMAP; MF_00605; -; 1. DR InterPro; IPR016009; tRNA_m1G_MeTrfase. DR InterPro; IPR002649; tRNA_m1G_MeTrfase_bac. DR Pfam; PF01746; tRNA_m1G_MT; 1. DR PIRSF; PIRSF000386; tRNA_mtase; 1. DR ProDom; PD004978; tRNA_m1G_mtfrase; 1. DR TIGRFAMs; TIGR00088; trmD; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 262 tRNA (guanine-N(1)-)-methyltransferase. FT /FTId=PRO_0000060347. FT REGION 149 154 S-adenosyl-L-methionine binding (By FT similarity). FT BINDING 129 129 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). SQ SEQUENCE 262 AA; 30500 MW; 653A65B1663A04CA CRC64; MELNKHDQTK TKYDNTLIWF CIITIFPEMF YAITNYGVTG KAIRKNIINI KFFNPRDFTD NKYKSVDDRP YGGGPGMLMS AKPLYLAIKN AKNLLKSAIV IYLSPQGKRL NQKKILEIIK NKKIIFVCGR YEGIDQRIID CQVDEEWSIG DYILTGGELA AMVAIDSISR FIPGVIKKKQ SVQEDSFFNG LLDYPHYTRP KIIEKMKVPE ILLSGNHDKI RLWRLKKSLE KTWTKRPDLL KNKILKKEEK ILLNELKKIN KR //