ID Q5U4E4_RAT Unreviewed; 440 AA. AC Q5U4E4; F1MAP8; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 22-FEB-2023, entry version 119. DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|PROSITE-ProRule:PRU00958}; DE EC=2.1.1.216 {ECO:0000256|PROSITE-ProRule:PRU00958}; GN Name=Trmt1 {ECO:0000313|EMBL:AAH85126.1, ECO:0000313|RGD:1305992}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH85126.1}; RN [1] {ECO:0000313|EMBL:AAH85126.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis {ECO:0000313|EMBL:AAH85126.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] {ECO:0007829|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00958}; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC085126; AAH85126.1; -; mRNA. DR RefSeq; NP_001013892.1; NM_001013870.1. DR AlphaFoldDB; Q5U4E4; -. DR PeptideAtlas; Q5U4E4; -. DR GeneID; 288914; -. DR KEGG; rno:288914; -. DR AGR; RGD:1305992; -. DR CTD; 55621; -. DR RGD; 1305992; Trmt1. DR HOGENOM; CLU_010862_4_1_1; -. DR InParanoid; Q5U4E4; -. DR OrthoDB; 942596at2759; -. DR PhylomeDB; Q5U4E4; -. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; ISO:RGD. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR002905; Trm1. DR PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1. DR PANTHER; PTHR10631:SF3; TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE; 1. DR Pfam; PF02005; TRM; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR TIGRFAMs; TIGR00308; TRM1; 1. DR PROSITE; PS51626; SAM_MT_TRM1; 1. PE 1: Evidence at protein level; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE- KW ProRule:PRU00958}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE- KW ProRule:PRU00958}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, KW ECO:0000256|PROSITE-ProRule:PRU00958}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00958}; tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE- KW ProRule:PRU00958}. FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 440 AA; 47643 MW; 366D8A67FC125461 CRC64; MERKAQEPPS PPTMENGTRS CEERPPAAPV ATVTEGAARI SFPSANEVFY NPVQEFNRDL TCAVITEFAR IHLGAKGIQI KVPGEKDLQK IAVDLSDQEE ETAGQNENLA PGDQPRTAAV GEICQEGLRV LEGLAASGLR SIRFALEVPG LQSVVANDAS ARAVELMHRN VELNGVAHLV QPNQADARML MYQHQKASER FDVIDLDPYG SPAPFLDAAV QAVSDGGLLC VTCTDMAVLA GNSGETCYSK YGAMALKSRA CHEMALRIVL HSLDLHANCY QRYIVPLLSI SADFYVRVFV RVFTGQAKVK SSASKQALVF QCVGCGAFYL QRLGKASGDP GGRVKFSAAC GPPVSPECEH CGQRHQLGGP MWAEPIHDLD FVGQVLEAVT TNPGRFHTST RIQGVLSVVT EELPDVPLYY TLDQLSSTVH CNTPRLLQLR //