TRMO_MOUSE
ID TRMO_MOUSE Reviewed; 431 AA.
AC Q562D6; Q3U5H3; Q8BRJ8; Q9D3F5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=tRNA (adenine(37)-N6)-methyltransferase;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9BU70};
DE AltName: Full=tRNA methyltransferase O {ECO:0000312|MGI:MGI:1922003};
GN Name=Trmo {ECO:0000312|MGI:MGI:1922003};
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase
CC responsible for the addition of the methyl group in the formation of
CC N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of
CC the tRNA anticodon loop of tRNA(Ser)(GCU). The methyl group of
CC m(6)t(6)A37 may improve the efficiency of the tRNA decoding ability.
CC May bind to tRNA. {ECO:0000250|UniProtKB:P28634,
CC ECO:0000250|UniProtKB:Q9BU70}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-
CC methionine = H(+) + N(6)-methyl,N(6)-L-threonylcarbamoyladenosine(37)
CC in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70027, Rhea:RHEA-
CC COMP:10163, Rhea:RHEA-COMP:17808, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74418,
CC ChEBI:CHEBI:188470; Evidence={ECO:0000250|UniProtKB:Q9BU70};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70028;
CC Evidence={ECO:0000250|UniProtKB:Q9BU70};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q562D6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q562D6-2; Sequence=VSP_025816;
CC Name=3;
CC IsoId=Q562D6-3; Sequence=VSP_025815;
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tRNA methyltransferase O family.
CC {ECO:0000305}.
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DR EMBL; AK017931; BAB31009.1; -; mRNA.
DR EMBL; AK044073; BAC31763.1; -; mRNA.
DR EMBL; AK153576; BAE32105.1; -; mRNA.
DR EMBL; AL806523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092543; AAH92543.1; -; mRNA.
DR CCDS; CCDS18148.1; -. [Q562D6-2]
DR CCDS; CCDS84727.1; -. [Q562D6-1]
DR RefSeq; NP_001334024.1; NM_001347095.1. [Q562D6-1]
DR RefSeq; NP_083362.1; NM_029086.2. [Q562D6-2]
DR AlphaFoldDB; Q562D6; -.
DR BioGRID; 216996; 1.
DR IntAct; Q562D6; 1.
DR MINT; Q562D6; -.
DR STRING; 10090.ENSMUSP00000083752; -.
DR iPTMnet; Q562D6; -.
DR PhosphoSitePlus; Q562D6; -.
DR EPD; Q562D6; -.
DR MaxQB; Q562D6; -.
DR PaxDb; Q562D6; -.
DR PRIDE; Q562D6; -.
DR ProteomicsDB; 298131; -. [Q562D6-1]
DR ProteomicsDB; 298132; -. [Q562D6-2]
DR ProteomicsDB; 298133; -. [Q562D6-3]
DR Antibodypedia; 28898; 168 antibodies from 27 providers.
DR Ensembl; ENSMUST00000030015; ENSMUSP00000030015; ENSMUSG00000028331. [Q562D6-1]
DR Ensembl; ENSMUST00000086563; ENSMUSP00000083752; ENSMUSG00000028331. [Q562D6-2]
DR GeneID; 74753; -.
DR KEGG; mmu:74753; -.
DR UCSC; uc008stp.1; mouse. [Q562D6-2]
DR UCSC; uc008stq.1; mouse. [Q562D6-1]
DR CTD; 51531; -.
DR MGI; MGI:1922003; Trmo.
DR VEuPathDB; HostDB:ENSMUSG00000028331; -.
DR eggNOG; KOG2942; Eukaryota.
DR GeneTree; ENSGT00390000004643; -.
DR HOGENOM; CLU_013458_1_0_1; -.
DR InParanoid; Q562D6; -.
DR OMA; YRRKHCQ; -.
DR OrthoDB; 1483097at2759; -.
DR TreeFam; TF331670; -.
DR BioGRID-ORCS; 74753; 2 hits in 39 CRISPR screens.
DR PRO; PR:Q562D6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q562D6; protein.
DR Bgee; ENSMUSG00000028331; Expressed in spermatocyte and 154 other tissues.
DR ExpressionAtlas; Q562D6; baseline and differential.
DR Genevisible; Q562D6; MM.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0089715; F:tRNA m6t6A37 methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR CDD; cd09281; UPF0066; 1.
DR Gene3D; 2.40.30.70; -; 1.
DR InterPro; IPR023370; TrmO-like_N.
DR InterPro; IPR023368; UPF0066_cons_site.
DR InterPro; IPR040372; YaeB-like.
DR InterPro; IPR036413; YaeB-like_sf.
DR InterPro; IPR036414; YaeB_N_sf.
DR PANTHER; PTHR12818; PTHR12818; 1.
DR Pfam; PF01980; TrmO; 1.
DR SUPFAM; SSF118196; SSF118196; 2.
DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1.
DR PROSITE; PS01318; TSAA_1; 1.
DR PROSITE; PS51668; TSAA_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..431
FT /note="tRNA (adenine(37)-N6)-methyltransferase"
FT /id="PRO_0000288887"
FT DOMAIN 30..168
FT /note="TsaA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01003"
FT REGION 196..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..49
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 90..91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 148..151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT VAR_SEQ 1..25
FT /note="MRGLEKQGSCATAAPCGCVQPALEA -> MWVRSAGPG (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025815"
FT VAR_SEQ 419..431
FT /note="VADPEESLAALGS -> TVLPPSPSPNGREEQSSVEEEVQQRAGPSRRAAPR
FT AASMLLTPQSSSLATSALTHWAISLPPLPQGLVFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025816"
FT CONFLICT 22
FT /note="A -> V (in Ref. 3; AAH92543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 47559 MW; 5C98C96BE6A6692B CRC64;
MRGLEKQGSC ATAAPCGCVQ PALEAGNLLT EPIGYLESCF PAKIGTPRQP SICSHSRACL
KIRKNIFNNP EHSLMGLEEF SHVWILFVFH KNGHLNYKAK VQPPRLNGAK TGVFSTRSPH
RPNAIGLTLA KLEKVEGGAV YLSGVDMIDG TPVLDIKPYI ADYDSPQNLS VHNDHHKLRA
EAQVDGTANS CDQLLLSGRG KVQPRQSTKE RPKCLEDRTS GENSQKSRDM SEIQHTLPED
RERALDLALE PSRGESMDMP ENQLGPPELK SFLEEGTDRP RKVEGALVLP GSSAETQWDA
SYRARTADRV PYSVVPSWVT EAPVAPLQVR FTPHAEMDLR KLNSGDASQP SFKYFHSAEE
AKRAIEAVLS ADPRSVYRRK LCEDRLFFFT VDTAHVTCWF GDGFAEVVRI KLASESVQVA
DPEESLAALG S
