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Protein

tRNA (guanine(26)-N(2))-dimethyltransferase

Gene

Trmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

2 S-adenosyl-L-methionine + guanine(26) in tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in tRNA.PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri599 – 62628C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, S-adenosyl-L-methionine, tRNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine(26)-N(2))-dimethyltransferase (EC:2.1.1.216)
Alternative name(s):
tRNA 2,2-dimethylguanosine-26 methyltransferase
tRNA(guanine-26,N(2)-N(2)) methyltransferase
tRNA(m(2,2)G26)dimethyltransferase
Gene namesi
Name:Trmt1
Synonyms:D8Ertd812e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1289155. Trmt1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663tRNA (guanine(26)-N(2))-dimethyltransferasePRO_0000147672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei516 – 5161PhosphoserineBy similarity
Modified residuei624 – 6241PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3TX08.
MaxQBiQ3TX08.
PaxDbiQ3TX08.
PeptideAtlasiQ3TX08.
PRIDEiQ3TX08.

PTM databases

iPTMnetiQ3TX08.
PhosphoSiteiQ3TX08.

Expressioni

Gene expression databases

BgeeiQ3TX08.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001974.

Structurei

3D structure databases

ProteinModelPortaliQ3TX08.
SMRiQ3TX08. Positions 155-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 498443Trm1 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.PROSITE-ProRule annotation
Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 Trm1 methyltransferase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri599 – 62628C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1253. Eukaryota.
COG1867. LUCA.
HOGENOMiHOG000177995.
HOVERGENiHBG000477.
InParanoidiQ3TX08.
KOiK00555.
OrthoDBiEOG7ZD1V0.
PhylomeDBiQ3TX08.
TreeFamiTF300851.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
4.10.1000.10. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 3 hits.
SSF90229. SSF90229. 1 hit.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3TX08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLARTILWL SRPLRPAHSL CRAQFMERKA QKPPSPPAME NGTRFCEERP
60 70 80 90 100
PADPVATVTE GAAKIVFPSA NEVFYNPVQE FNRDLTCAVI TEFARIHLGA
110 120 130 140 150
KGIQIKVPGE KDSEKIAVDL SDQEEETAGK NENLAPGDWP RTAAVGEICE
160 170 180 190 200
EGLRVLEGLA ASGLRSIRFA LEVPGLQSVV ANDASARAVE LMHRNVELNG
210 220 230 240 250
VAHLVQPNQA DARMLMYQHQ KAPERFDVID LDPYGSPAPF LDAAVQAVSD
260 270 280 290 300
GGLLCVTCTD MAVLAGNSGE TCYSKYGAMA LKSRACHEMA LRIVLHSLDL
310 320 330 340 350
HANCYQRYIV PLLSISADFY IRVFVRVFTG QAKVKSSASK QALVFQCVGC
360 370 380 390 400
GAFYLQRLGK ASGDPGGRIK FSAACGPPVT PECEHCGQRH QLGGPMWAEP
410 420 430 440 450
IHDLDFVGRV LDAVTTNPGR FHTSMRIQGV LSVVTEELPD VPLYYTLDQL
460 470 480 490 500
SSTIHCNTPR LLQLRSALLH AGFRVSLSHA CKNAVKTDAP PEALWDIMRC
510 520 530 540 550
WEKECPVKRE RLSESSPAFR ILAVEPRLKA NFNIREDANP SSRQRGLKRF
560 570 580 590 600
QANPEANWGP RPRARPGGKA ASEDLAGRRR LLQNKRKEPA EDPAQRAARL
610 620 630 640 650
KTFPCKRFKE GTCQLGDQCC YSHSPAAPVA SGDIPIEECP ETTTKISPGP
660
KAAAGGIPGP GVD
Length:663
Mass (Da):72,350
Last modified:December 20, 2005 - v2
Checksum:i28D9D7678FED5D55
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462FC → SW in BAE35108 (PubMed:16141072).Curated
Sequence conflicti112 – 1121D → E in BAE42173 (PubMed:16141072).Curated
Sequence conflicti175 – 1751G → D in BAE42173 (PubMed:16141072).Curated
Sequence conflicti656 – 6561G → V in BAE42173 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159467 mRNA. Translation: BAE35108.1.
AK171002 mRNA. Translation: BAE42173.1.
CCDSiCCDS40410.2.
RefSeqiNP_001158031.1. NM_001164559.1.
NP_001158032.1. NM_001164560.1.
NP_932137.2. NM_198020.2.
UniGeneiMm.275720.

Genome annotation databases

GeneIDi212528.
KEGGimmu:212528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159467 mRNA. Translation: BAE35108.1.
AK171002 mRNA. Translation: BAE42173.1.
CCDSiCCDS40410.2.
RefSeqiNP_001158031.1. NM_001164559.1.
NP_001158032.1. NM_001164560.1.
NP_932137.2. NM_198020.2.
UniGeneiMm.275720.

3D structure databases

ProteinModelPortaliQ3TX08.
SMRiQ3TX08. Positions 155-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001974.

PTM databases

iPTMnetiQ3TX08.
PhosphoSiteiQ3TX08.

Proteomic databases

EPDiQ3TX08.
MaxQBiQ3TX08.
PaxDbiQ3TX08.
PeptideAtlasiQ3TX08.
PRIDEiQ3TX08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi212528.
KEGGimmu:212528.

Organism-specific databases

CTDi55621.
MGIiMGI:1289155. Trmt1.

Phylogenomic databases

eggNOGiKOG1253. Eukaryota.
COG1867. LUCA.
HOGENOMiHOG000177995.
HOVERGENiHBG000477.
InParanoidiQ3TX08.
KOiK00555.
OrthoDBiEOG7ZD1V0.
PhylomeDBiQ3TX08.
TreeFamiTF300851.

Miscellaneous databases

ChiTaRSiTrmt1. mouse.
PROiQ3TX08.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TX08.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
4.10.1000.10. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 3 hits.
SSF90229. SSF90229. 1 hit.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiTRM1_MOUSE
AccessioniPrimary (citable) accession number: Q3TX08
Secondary accession number(s): Q3TBY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 6, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.