ID TRM10_YEAST Reviewed; 293 AA. AC Q12400; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase TRM10; DE Short=tRNA methyltransferase 10; DE EC=2.1.1.31; GN Name=TRM10; OrderedLocusNames=YOL093W; ORFNames=O0926; 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 [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=96021609; PubMed=8533473; DOI=10.1002/yea.320111009; RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.; RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains RT more than twice as many unknown as known open reading frames."; RL Yeast 11:975-986(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313270; PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., RA Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., RA Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., RA Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., RA Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., RA Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., RA Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., RA Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., RA Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., RA Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., RA Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., RA Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., RA Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., RA Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., RA Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). 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 FUNCTION. RX MEDLINE=22588906; PubMed=12702816; DOI=10.1261/rna.5070303; RA Jackman J.E., Montange R.K., Malik H.S., Phizicky E.M.; RT "Identification of the yeast gene encoding the tRNA m1G RT methyltransferase responsible for modification at position 9."; RL RNA 9:574-585(2003). RN [6] RP FUNCTION. RX PubMed=15640439; DOI=10.1093/nar/gni002; RA Hiley S.L., Jackman J.E., Babak T., Trochesset M., Morris Q.D., RA Phizicky E.M., Hughes T.R.; RT "Detection and discovery of RNA modifications using microarrays."; RL Nucleic Acids Res. 33:E2-E2(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-16, 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). CC -!- FUNCTION: Catalyzes the formation of N(1)-methylguanine at CC position 9 (m1G9) in cytoplasmic tRNAs. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L- CC homocysteine + tRNA containing N(1)-methylguanine. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-29692, EBI-29692; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- MISCELLANEOUS: Present with 4090 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the RNA methyltransferase trmD family. CC TRM10 subfamily. 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; X83121; CAA58186.1; -; Genomic_DNA. DR EMBL; Z74835; CAA99105.1; -; Genomic_DNA. DR PIR; S57376; S57376. DR RefSeq; NP_014548.1; -. DR DIP; DIP:4737N; -. DR IntAct; Q12400; 3. DR Ensembl; YOL093W; Saccharomyces cerevisiae. DR GeneID; 854060; -. DR GenomeReviews; Y13140_GR; YOL093W. DR KEGG; sce:YOL093W; -. DR NMPDR; fig|4932.3.peg.5637; -. DR CYGD; YOL093w; -. DR SGD; S000005453; TRM10. DR HOGENOM; Q12400; -. DR OMA; Q12400; RKRIRRD. DR BRENDA; 2.1.1.31; 250. DR NextBio; 975659; -. DR ArrayExpress; Q12400; -. DR GermOnline; YOL093W; Saccharomyces cerevisiae. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IEA:EC. DR GO; GO:0030488; P:tRNA methylation; IDA:SGD. DR InterPro; IPR016009; tRNA_m1G_MeTrfase. DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk. DR InterPro; IPR016653; tRNA_m1G_mtfrase_met. DR PANTHER; PTHR13563; DUF425; 1. DR Pfam; PF01746; tRNA_m1G_MT; 1. DR PIRSF; PIRSF016323; tRNA_m1G_mtfrase_met; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Methyltransferase; Nucleus; KW Phosphoprotein; S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 293 tRNA (guanine-N(1)-)-methyltransferase FT TRM10. FT /FTId=PRO_0000060520. FT MOD_RES 2 2 Phosphoserine. FT MOD_RES 16 16 Phosphothreonine. SQ SEQUENCE 293 AA; 34520 MW; C3DC7C4BB2FFBE63 CRC64; MSNDEINQNE EKVKRTPPLP PVPEGMSKKQ WKKMCKRQRW EENKAKYNAE RRVKKKRLRH ERSAKIQEYI DRGEEVPQEL IREPRINVNQ TDSGIEIILD CSFDELMNDK EIVSLSNQVT RAYSANRRAN HFAEIKVAPF DKRLKQRFET TLKNTNYENW NHFKFLPDDK IMFGDEHISK DKIVYLTADT EEKLEKLEPG MRYIVGGIVD KNRYKELCLK KAQKMGIPTR RLPIDEYINL EGRRVLTTTH VVQLMLKYFD DHNWKNAFES VLPPRKLDAE AKSASSSPAP KDT //