ID TRMD_BACTN Reviewed; 225 AA. AC Q8A9C2; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 16-JUN-2009, entry version 44. 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=BT_0893; OS Bacteroides thetaiotaomicron. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=818; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482; RX MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., RA Chiang H.C., Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). 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; AE015928; AAO76000.1; -; Genomic_DNA. DR RefSeq; NP_809806.1; -. DR GeneID; 1073262; -. DR GenomeReviews; AE015928_GR; BT_0893. DR KEGG; bth:BT_0893; -. DR NMPDR; fig|226186.1.peg.893; -. DR HOGENOM; Q8A9C2; -. DR OMA; Q8A9C2; HRSVDDT. DR BioCyc; BTHE226186:BT_0893-MON; -. DR BRENDA; 2.1.1.31; 21018. 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 1 225 tRNA (guanine-N(1)-)-methyltransferase. FT /FTId=PRO_0000060330. FT REGION 132 137 S-adenosyl-L-methionine binding (By FT similarity). FT BINDING 112 112 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). SQ SEQUENCE 225 AA; 25558 MW; 0B49CF62E2AC9E71 CRC64; MRIDIITVLP EMIEGFFNCS IMKRAQNKGL AEIHIHNLRD YTEDKYRRVD DYPFGGFAGM VMKIEPIERC INALKAERDY DEVIFTTPDG EQFNQPMANS LSLAQNLIIL CGHFKGIDYR IREHLITKEI SIGDYVLTGG ELAAAVMADA IVRIIPGVIS DEQSALSDSF QDNLLAAPVY TRPADYKGWK VPDILLSGHE AKIKEWELQQ SLERTKKLRP DLLED //