TRM1_MOUSE
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 03-AUG-2022, entry version 119.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase;
DE EC=2.1.1.216;
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase;
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) 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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of most
CC tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
CC {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00958};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|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; AK159467; BAE35108.1; -; mRNA.
DR EMBL; AK171002; BAE42173.1; -; mRNA.
DR CCDS; CCDS40410.2; -.
DR RefSeq; NP_001158031.1; NM_001164559.1.
DR RefSeq; NP_001158032.1; NM_001164560.1.
DR RefSeq; NP_932137.2; NM_198020.2.
DR AlphaFoldDB; Q3TX08; -.
DR SMR; Q3TX08; -.
DR BioGRID; 229336; 25.
DR STRING; 10090.ENSMUSP00000001974; -.
DR iPTMnet; Q3TX08; -.
DR PhosphoSitePlus; Q3TX08; -.
DR EPD; Q3TX08; -.
DR jPOST; Q3TX08; -.
DR MaxQB; Q3TX08; -.
DR PaxDb; Q3TX08; -.
DR PeptideAtlas; Q3TX08; -.
DR PRIDE; Q3TX08; -.
DR ProteomicsDB; 298130; -.
DR GeneID; 212528; -.
DR KEGG; mmu:212528; -.
DR CTD; 55621; -.
DR MGI; MGI:1289155; Trmt1.
DR eggNOG; KOG1253; Eukaryota.
DR InParanoid; Q3TX08; -.
DR OrthoDB; 1414511at2759; -.
DR PhylomeDB; Q3TX08; -.
DR TreeFam; TF300851; -.
DR BioGRID-ORCS; 212528; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Trmt1; mouse.
DR PRO; PR:Q3TX08; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3TX08; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.30.56.70; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR10631; PTHR10631; 1.
DR Pfam; PF02005; TRM; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR TIGRFAMs; TIGR00308; TRM1; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Methyltransferase; Phosphoprotein; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing;
KW tRNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..663
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_0000147672"
FT DOMAIN 56..498
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT ZN_FING 599..626
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 534..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXH9"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXH9"
FT CONFLICT 45..46
FT /note="FC -> SW (in Ref. 1; BAE35108)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="D -> E (in Ref. 1; BAE42173)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="G -> D (in Ref. 1; BAE42173)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="G -> V (in Ref. 1; BAE42173)"
FT /evidence="ECO:0000305"
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
