ID TRM1_MOUSE Reviewed; 663 AA. AC Q3TX08; Q3TBY4; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 16-JUN-2009, entry version 32. 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=Trmt1; Synonyms=D8Ertd812e; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=17203969; DOI=10.1021/pr0604155; RA Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; RT "Protein phosphorylation and expression profiling by Yin-yang RT multidimensional liquid chromatography (Yin-yang MDLC) mass RT spectrometry."; RL J. Proteome Res. 6:250-262(2007). CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of CC most tRNAs using S-adenosyl-L-methionine as donor of the methyl CC 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 -!- SIMILARITY: Contains 1 C3H1-type zinc finger. 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; AK159467; BAE35108.1; -; mRNA. DR EMBL; AK171002; BAE42173.1; -; mRNA. DR IPI; IPI00321152; -. DR UniGene; Mm.275720; -. DR PhosphoSite; Q3TX08; -. DR Ensembl; ENSMUSG00000001909; Mus musculus. DR MGI; MGI:1289155; Trmt1. DR HOGENOM; Q3TX08; -. DR HOVERGEN; Q3TX08; -. DR BRENDA; 2.1.1.32; 244. DR ArrayExpress; Q3TX08; -. DR Bgee; Q3TX08; -. DR GermOnline; ENSMUSG00000001909; Mus musculus. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR InterPro; IPR002905; TRM_MeTrfase. DR InterPro; IPR000571; Znf_CCCH. DR PANTHER; PTHR10631; TRM_mtfrase; 1. DR Pfam; PF02005; TRM; 1. DR Pfam; PF00642; zf-CCCH; 1. DR SMART; SM00356; ZnF_C3H1; 1. DR TIGRFAMs; TIGR00308; TRM1; 1. DR PROSITE; PS50103; ZF_C3H1; 1. PE 1: Evidence at protein level; KW Metal-binding; Methyltransferase; Phosphoprotein; KW S-adenosyl-L-methionine; Transferase; tRNA processing; Zinc; KW Zinc-finger. FT CHAIN 1 663 N(2),N(2)-dimethylguanosine tRNA FT methyltransferase. FT /FTId=PRO_0000147672. FT ZN_FING 599 626 C3H1-type. FT MOD_RES 121 121 Phosphoserine. FT MOD_RES 624 624 Phosphoserine (By similarity). FT CONFLICT 45 46 FC -> SW (in Ref. 1; BAE35108). FT CONFLICT 112 112 D -> E (in Ref. 1; BAE42173). FT CONFLICT 175 175 G -> D (in Ref. 1; BAE42173). FT CONFLICT 656 656 G -> V (in Ref. 1; BAE42173). SQ SEQUENCE 663 AA; 72350 MW; 28D9D7678FED5D55 CRC64; MSLARTILWL SRPLRPAHSL CRAQFMERKA QKPPSPPAME NGTRFCEERP PADPVATVTE GAAKIVFPSA NEVFYNPVQE FNRDLTCAVI TEFARIHLGA KGIQIKVPGE KDSEKIAVDL SDQEEETAGK NENLAPGDWP RTAAVGEICE EGLRVLEGLA ASGLRSIRFA LEVPGLQSVV ANDASARAVE LMHRNVELNG VAHLVQPNQA DARMLMYQHQ KAPERFDVID LDPYGSPAPF LDAAVQAVSD GGLLCVTCTD MAVLAGNSGE TCYSKYGAMA LKSRACHEMA LRIVLHSLDL HANCYQRYIV PLLSISADFY IRVFVRVFTG QAKVKSSASK QALVFQCVGC GAFYLQRLGK ASGDPGGRIK FSAACGPPVT PECEHCGQRH QLGGPMWAEP IHDLDFVGRV LDAVTTNPGR FHTSMRIQGV LSVVTEELPD VPLYYTLDQL SSTIHCNTPR LLQLRSALLH AGFRVSLSHA CKNAVKTDAP PEALWDIMRC WEKECPVKRE RLSESSPAFR ILAVEPRLKA NFNIREDANP SSRQRGLKRF QANPEANWGP RPRARPGGKA ASEDLAGRRR LLQNKRKEPA EDPAQRAARL KTFPCKRFKE GTCQLGDQCC YSHSPAAPVA SGDIPIEECP ETTTKISPGP KAAAGGIPGP GVD //