Reviewed, UniProtKB/Swiss-Prot Q3TX08 (TRM1_MOUSE)

Names and origin

Protein names

Recommended name:
    N(2),N(2)-dimethylguanosine tRNA methyltransferase
    EC=2.1.1.32
Alternative name(s):
    tRNA(guanine-26,N(2)-N(2)) methyltransferase
    tRNA 2,2-dimethylguanosine-26 methyltransferase
    tRNA(m(2,2)G26)dimethyltransferase

Gene names

Name:	Trmt1
Synonyms:	D8Ertd812e

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups By similarity.
Catalytic activity	S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(2)-methylguanine.
Sequence similarities	Belongs to the TRM1 family. Contains 1 C3H1-type zinc finger.

Ontologies

Keywords
Biological process	tRNA processing
Domain	Zinc-finger
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro tRNA (guanine-N2-)-methyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 663	663	N(2),N(2)-dimethylguanosine tRNA methyltransferase		PRO_0000147672
Regions
	Zinc finger	599 – 626	28	C3H1-type
Amino acid modifications
	Modified residue	121	1	Phosphoserine Ref.2
	Modified residue	624	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	45 – 46	2	FC → SW in BAE35108. Ref.1
	Sequence conflict	112	1	D → E in BAE42173. Ref.1
	Sequence conflict	175	1	G → D in BAE42173. Ref.1
	Sequence conflict	656	1	G → V in BAE42173. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q3TX08-1 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: 28D9D7678FED5D55	FASTA	663	72,350
	10 20 30 40 50 60 MSLARTILWL SRPLRPAHSL CRAQFMERKA QKPPSPPAME NGTRFCEERP PADPVATVTE 70 80 90 100 110 120 GAAKIVFPSA NEVFYNPVQE FNRDLTCAVI TEFARIHLGA KGIQIKVPGE KDSEKIAVDL 130 140 150 160 170 180 SDQEEETAGK NENLAPGDWP RTAAVGEICE EGLRVLEGLA ASGLRSIRFA LEVPGLQSVV 190 200 210 220 230 240 ANDASARAVE LMHRNVELNG VAHLVQPNQA DARMLMYQHQ KAPERFDVID LDPYGSPAPF 250 260 270 280 290 300 LDAAVQAVSD GGLLCVTCTD MAVLAGNSGE TCYSKYGAMA LKSRACHEMA LRIVLHSLDL 310 320 330 340 350 360 HANCYQRYIV PLLSISADFY IRVFVRVFTG QAKVKSSASK QALVFQCVGC GAFYLQRLGK 370 380 390 400 410 420 ASGDPGGRIK FSAACGPPVT PECEHCGQRH QLGGPMWAEP IHDLDFVGRV LDAVTTNPGR 430 440 450 460 470 480 FHTSMRIQGV LSVVTEELPD VPLYYTLDQL SSTIHCNTPR LLQLRSALLH AGFRVSLSHA 490 500 510 520 530 540 CKNAVKTDAP PEALWDIMRC WEKECPVKRE RLSESSPAFR ILAVEPRLKA NFNIREDANP 550 560 570 580 590 600 SSRQRGLKRF QANPEANWGP RPRARPGGKA ASEDLAGRRR LLQNKRKEPA EDPAQRAARL 610 620 630 640 650 660 KTFPCKRFKE GTCQLGDQCC YSHSPAAPVA SGDIPIEECP ETTTKISPGP KAAAGGIPGP GVD

References

[1]

"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD.

[2]

"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, MASS SPECTROMETRY. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK159467 mRNA. Translation: BAE35108.1. AK171002 mRNA. Translation: BAE42173.1.
IPI	IPI00321152.
UniGene	Mm.275720
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q3TX08.
Genome annotation databases
Ensembl	ENSMUSG00000001909. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:1289155. Trmt1.
Phylogenomic databases
HOGENOM	Q3TX08.
HOVERGEN	Q3TX08.
Enzyme and pathway databases
BRENDA	2.1.1.32. 244.
Gene expression databases
ArrayExpress	Q3TX08.
Bgee	Q3TX08.
GermOnline	ENSMUSG00000001909. Mus musculus.
Family and domain databases
InterPro	IPR002905. TRM_MeTrfase. IPR000571. Znf_CCCH. [Graphical view]
PANTHER	PTHR10631. TRM_mtfrase. 1 hit.
Pfam	PF02005. TRM. 1 hit. PF00642. zf-CCCH. 1 hit. [Graphical view]
SMART	SM00356. ZnF_C3H1. 1 hit. [Graphical view]
TIGRFAMs	TIGR00308. TRM1. 1 hit.
PROSITE	PS50103. ZF_C3H1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

TRM1_MOUSE

Accession

Primary (citable) accession number: Q3TX08
Secondary accession number(s): Q3TBY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	June 16, 2009
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)