ID TRM1_METMA Reviewed; 388 AA. AC Q8PU28; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 38. DE RecName: Full=N(2),N(2)-dimethylguanosine tRNA methyltransferase; DE EC=2.1.1.32; DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase; DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase; DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase; GN Name=trm1; OrderedLocusNames=MM_2528; OS Methanosarcina mazei (Methanosarcina frisia). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=2209; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88; RX MEDLINE=22120827; PubMed=12125824; RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., RA Fritz H.-J., Gottschalk G.; RT "The genome of Methanosarcina mazei: evidence for lateral gene RT transfer between Bacteria and Archaea."; RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002). CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of CC a number of tRNAs using S-adenosyl-L-methionine as donor of the CC methyl groups (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L- CC homocysteine + tRNA containing N(2)-methylguanine. CC -!- SIMILARITY: Belongs to the TRM1 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; AE008384; AAM32224.1; -; Genomic_DNA. DR RefSeq; NP_634552.1; -. DR GeneID; 1480870; -. DR GenomeReviews; AE008384_GR; MM_2528. DR KEGG; mma:MM_2528; -. DR NMPDR; fig|192952.1.peg.2528; -. DR HOGENOM; Q8PU28; -. DR OMA; Q8PU28; MELNRDI. DR BioCyc; MMAZ192952:MM2528-MON; -. DR BRENDA; 2.1.1.32; 261165. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:HAMAP. DR HAMAP; MF_00290; -; 1. DR InterPro; IPR002905; TRM_MeTrfase. DR PANTHER; PTHR10631; TRM_mtfrase; 1. DR Pfam; PF02005; TRM; 1. DR TIGRFAMs; TIGR00308; TRM1; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1 388 N(2),N(2)-dimethylguanosine tRNA FT methyltransferase. FT /FTId=PRO_0000147684. SQ SEQUENCE 388 AA; 42784 MW; F3796A5EC7820DD3 CRC64; MICRTIVEGT TKISVPVPPP DANFPPSAAP VFYNPEMELN RDINVAATAA FVERLLSKKD ILREEIRYVD AFSASGIRGL RIAGEVGIHS TMNDWSHEAF ELIKENIKIN GLEEKAQATR RNANVLLHEQ RFHIVDVDPF GTPSPYLDAA ASSAYSMLSV TATDTAPLCG AHLNSGIRKY ASVPLNTEYH SEMGLRVLLG ACARELAKHE KGMLPLLSHV TRHYVRTYLE VLPGSRKADK TLKSMGFVAH CPRCGFRKPV YGLAVHIEKE CPECGGLTKI AGPLWLGPYR EPEFCNEVIS ELEAHPLNTK EKVRKIITFC RDELDIPMFY DQHVICKELG ASATGIESLI EALRAGGFEA SRTHFTGTSF KTDAPIAEIK KIILALSG //