ID TRMB_YEAST Reviewed; 286 AA. AC Q12009; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 69. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase; DE EC=2.1.1.33; DE AltName: Full=tRNA(m7G46)-methyltransferase; DE AltName: Full=Transfer RNA methyltransferase 8; GN Name=TRM8; OrderedLocusNames=YDL201W; ORFNames=D1075; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313263; PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [2] RP CHARACTERIZATION, AND INTERACTION WITH TRM82. RX MEDLINE=22290633; PubMed=12403464; DOI=10.1017/S1355838202024019; RA Alexandrov A., Martzen M.R., Phizicky E.M.; RT "Two proteins that form a complex are required for 7-methylguanosine RT modification of yeast tRNA."; RL RNA 8:1253-1266(2002). RN [3] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP CATALYTIC ACTIVITY, TRNA-BINDING, AND INTERACTION WITH TRM82. RX PubMed=15811913; DOI=10.1261/rna.2030705; RA Alexandrov A., Grayhack E.J., Phizicky E.M.; RT "tRNA m7G methyltransferase Trm8p/Trm82p: evidence linking activity to RT a growth phenotype and implicating Trm82p in maintaining levels of RT active Trm8p."; RL RNA 11:821-830(2005). RN [6] RP FUNCTION. RX PubMed=16387656; DOI=10.1016/j.molcel.2005.10.036; RA Alexandrov A., Chernyakov I., Gu W., Hiley S.L., Hughes T.R., RA Grayhack E.J., Phizicky E.M.; RT "Rapid tRNA decay can result from lack of nonessential RT modifications."; RL Mol. Cell 21:87-96(2006). RN [7] RP FUNCTION. RX PubMed=17382321; DOI=10.1016/j.febslet.2007.03.023; RA Matsumoto K., Toyooka T., Tomikawa C., Ochi A., Takano Y., RA Takayanagi N., Endo Y., Hori H.; RT "RNA recognition mechanism of eukaryote tRNA (m7G46) methyltransferase RT (Trm8-Trm82 complex)."; RL FEBS Lett. 581:1599-1604(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASS RP SPECTROMETRY. RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS RP SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-37, AND MASS RP SPECTROMETRY. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-286 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND TRM82, SUBUNIT, AND PROBABLE ACTIVE SITE. RX PubMed=18184583; DOI=10.1016/j.str.2007.10.025; RA Leulliot N., Chaillet M., Durand D., Ulryck N., Blondeau K., RA van Tilbeurgh H.; RT "Structure of the yeast tRNA m7G methylation complex."; RL Structure 16:52-61(2008). CC -!- FUNCTION: Methyltransferase that catalyzes the formation of N(7)- CC methylguanine at position 46 (m7G46) in tRNA, a modification CC required to maintain stability of tRNAs; its absence resulting in CC tRNA decay. Both the D-stem and T-stem structures of tRNAs are CC required for efficient methyltransferase activity. 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: Forms a complex with TRM82. CC -!- INTERACTION: CC Q03774:TRM82; NbExp=1; IntAct=EBI-19552, EBI-19486; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 2630 molecules/cell in log phase SD CC medium. 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; X99000; CAA67468.1; -; Genomic_DNA. DR EMBL; Z74249; CAA98779.1; -; Genomic_DNA. DR PIR; S67760; S67760. DR RefSeq; NP_010080.1; -. DR PDB; 2VDU; X-ray; 2.40 A; E/F=39-286. DR PDB; 2VDV; X-ray; 2.30 A; E/F=47-286. DR PDBsum; 2VDU; -. DR PDBsum; 2VDV; -. DR DIP; DIP:8614N; -. DR IntAct; Q12009; 1. DR PeptideAtlas; Q12009; -. DR Ensembl; YDL201W; Saccharomyces cerevisiae. DR GeneID; 851326; -. DR GenomeReviews; Z71256_GR; YDL201W. DR KEGG; sce:YDL201W; -. DR NMPDR; fig|4932.3.peg.813; -. DR CYGD; YDL201w; -. DR SGD; S000002360; TRM8. DR HOGENOM; Q12009; -. DR OMA; Q12009; PDPHFKQ. DR BRENDA; 2.1.1.33; 250. DR NextBio; 968378; -. DR GermOnline; YDL201W; Saccharomyces cerevisiae. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:EC. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0030488; P:tRNA methylation; IDA:SGD. 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; Nucleus; KW Phosphoprotein; RNA-binding; S-adenosyl-L-methionine; Transferase; KW tRNA processing; tRNA-binding. FT CHAIN 1 286 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000171437. FT REGION 126 127 S-adenosyl-L-methionine binding. FT REGION 161 162 S-adenosyl-L-methionine binding. FT REGION 259 261 S-adenosyl-L-methionine binding. FT ACT_SITE 184 184 Probable. FT BINDING 103 103 S-adenosyl-L-methionine; via carbonyl FT oxygen. FT BINDING 181 181 S-adenosyl-L-methionine; via carbonyl FT oxygen. FT MOD_RES 7 7 Phosphoserine; by ATM or ATR. FT MOD_RES 37 37 Phosphoserine. FT MOD_RES 59 59 Phosphoserine. SQ SEQUENCE 286 AA; 33391 MW; 0280B9A7B02C85B7 CRC64; MKAKPLSQDP GSKRYAYRIN KEENRKELKH VKINESSLVQ EGQKIDLPKK RYYRQRAHSN PFSDHQLEYP VSPQDMDWSK LYPYYKNAEN GQMTKKVTIA DIGCGFGGLM IDLSPAFPED LILGMEIRVQ VTNYVEDRII ALRNNTASKH GFQNINVLRG NAMKFLPNFF EKGQLSKMFF CFPDPHFKQR KHKARIITNT LLSEYAYVLK EGGVVYTITD VKDLHEWMVK HLEEHPLFER LSKEWEENDE CVKIMRNATE EGKKVERKKG DKFVACFTRL PTPAIL //