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   24-JAN-2024, entry version 112.
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; 10090-ENSMUSP00000083752; -.
DR   ProteomicsDB; 298131; -. [Q562D6-1]
DR   ProteomicsDB; 298132; -. [Q562D6-2]
DR   ProteomicsDB; 298133; -. [Q562D6-3]
DR   Antibodypedia; 28898; 175 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000030015.6; ENSMUSP00000030015.6; ENSMUSG00000028331.13. [Q562D6-1]
DR   Ensembl; ENSMUST00000086563.11; ENSMUSP00000083752.5; ENSMUSG00000028331.13. [Q562D6-2]
DR   GeneID; 74753; -.
DR   KEGG; mmu:74753; -.
DR   UCSC; uc008stp.1; mouse. [Q562D6-2]
DR   UCSC; uc008stq.1; mouse. [Q562D6-1]
DR   AGR; MGI:1922003; -.
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; IDMIQGT; -.
DR   OrthoDB; 5477652at2759; -.
DR   TreeFam; TF331670; -.
DR   BioGRID-ORCS; 74753; 3 hits in 44 CRISPR screens.
DR   PRO; PR:Q562D6; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q562D6; Protein.
DR   Bgee; ENSMUSG00000028331; Expressed in spermatocyte and 157 other cell types or tissues.
DR   ExpressionAtlas; Q562D6; baseline and differential.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0089715; F:tRNA (L-threonylcarbamoyladenosine(37)-C2) methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR   CDD; cd09281; UPF0066; 1.
DR   Gene3D; 2.40.30.70; YaeB-like; 1.
DR   Gene3D; 3.30.2310.10; YaeB-like; 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   NCBIfam; TIGR00104; tRNA_TsaA; 1.
DR   PANTHER; PTHR12818:SF0; TRNA (ADENINE(37)-N6)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12818; UNCHARACTERIZED; 1.
DR   Pfam; PF01980; TrmO; 1.
DR   SUPFAM; SSF118196; YaeB-like; 2.
DR   PROSITE; PS01318; TSAA_1; 1.
DR   PROSITE; PS51668; TSAA_2; 1.
DR   Genevisible; Q562D6; MM.
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
//