ID TRMO_HUMAN Reviewed; 441 AA. AC Q9BU70; Q5T113; Q86SK0; Q9NXJ7; Q9P0Q7; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 24-JAN-2024, entry version 144. DE RecName: Full=tRNA (adenine(37)-N6)-methyltransferase {ECO:0000305}; DE EC=2.1.1.- {ECO:0000269|PubMed:25063302}; DE AltName: Full=tRNA methyltransferase O {ECO:0000303|PubMed:25063302, ECO:0000312|HGNC:HGNC:30967}; GN Name=TRMO {ECO:0000303|PubMed:25063302, ECO:0000312|HGNC:HGNC:30967}; GN Synonyms=C9orf156; ORFNames=HSPC219; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-7. RC TISSUE=Colon mucosa; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-7. RC TISSUE=Lung; 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). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-241. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-441. RC TISSUE=Lymphocyte; RX PubMed=9153233; DOI=10.1074/jbc.272.21.13779; RA Liu L.X., Margottin F., Le Gall S., Schwartz O., Selig L., Benarous R., RA Benichou S.; RT "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef- RT mediated CD4 down-regulation."; RL J. Biol. Chem. 272:13779-13785(1997). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25063302; DOI=10.1093/nar/gku618; RA Kimura S., Miyauchi K., Ikeuchi Y., Thiaville P.C., Crecy-Lagard V.D., RA Suzuki T.; RT "Discovery of the beta-barrel-type RNA methyltransferase responsible for RT N6-methylation of N6-threonylcarbamoyladenosine in tRNAs."; RL Nucleic Acids Res. 42:9350-9365(2014). 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) (PubMed:25063302). The methyl CC group of m(6)t(6)A37 may improve the efficiency of the tRNA decoding CC ability (By similarity). {ECO:0000250|UniProtKB:P28634, CC ECO:0000269|PubMed:25063302}. 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:0000305|PubMed:25063302}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70028; CC Evidence={ECO:0000305|PubMed:25063302}; CC -!- INTERACTION: CC Q9BU70; Q9H0A9-2: SPATC1L; NbExp=5; IntAct=EBI-2652818, EBI-11995806; CC -!- SIMILARITY: Belongs to the tRNA methyltransferase O family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF36139.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF36139.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305}; 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; AK000213; BAA91013.1; -; mRNA. DR EMBL; AL499604; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002863; AAH02863.1; -; mRNA. DR EMBL; AF151053; AAF36139.1; ALT_SEQ; mRNA. DR EMBL; X86033; CAA60025.1; -; mRNA. DR CCDS; CCDS6730.1; -. DR RefSeq; NP_001317654.1; NM_001330725.1. DR RefSeq; NP_057565.3; NM_016481.4. DR AlphaFoldDB; Q9BU70; -. DR BioGRID; 119593; 32. DR IntAct; Q9BU70; 28. DR MINT; Q9BU70; -. DR STRING; 9606.ENSP00000364260; -. DR GlyGen; Q9BU70; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BU70; -. DR PhosphoSitePlus; Q9BU70; -. DR BioMuta; TRMO; -. DR DMDM; 152112517; -. DR EPD; Q9BU70; -. DR MassIVE; Q9BU70; -. DR MaxQB; Q9BU70; -. DR PaxDb; 9606-ENSP00000364260; -. DR PeptideAtlas; Q9BU70; -. DR ProteomicsDB; 79058; -. DR Pumba; Q9BU70; -. DR Antibodypedia; 28898; 175 antibodies from 27 providers. DR DNASU; 51531; -. DR Ensembl; ENST00000375119.8; ENSP00000364260.3; ENSG00000136932.15. DR GeneID; 51531; -. DR KEGG; hsa:51531; -. DR MANE-Select; ENST00000375119.8; ENSP00000364260.3; NM_016481.5; NP_057565.3. DR UCSC; uc004axv.2; human. DR AGR; HGNC:30967; -. DR CTD; 51531; -. DR DisGeNET; 51531; -. DR GeneCards; TRMO; -. DR HGNC; HGNC:30967; TRMO. DR HPA; ENSG00000136932; Low tissue specificity. DR neXtProt; NX_Q9BU70; -. DR OpenTargets; ENSG00000136932; -. DR PharmGKB; PA134875112; -. DR VEuPathDB; HostDB:ENSG00000136932; -. DR eggNOG; KOG2942; Eukaryota. DR GeneTree; ENSGT00390000004643; -. DR HOGENOM; CLU_013458_1_0_1; -. DR InParanoid; Q9BU70; -. DR OMA; IDMIQGT; -. DR OrthoDB; 5477652at2759; -. DR PhylomeDB; Q9BU70; -. DR TreeFam; TF331670; -. DR PathwayCommons; Q9BU70; -. DR SignaLink; Q9BU70; -. DR BioGRID-ORCS; 51531; 12 hits in 1131 CRISPR screens. DR GenomeRNAi; 51531; -. DR Pharos; Q9BU70; Tbio. DR PRO; PR:Q9BU70; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9BU70; Protein. DR Bgee; ENSG00000136932; Expressed in epithelium of nasopharynx and 179 other cell types or tissues. DR ExpressionAtlas; Q9BU70; baseline and differential. DR GO; GO:0089715; F:tRNA (L-threonylcarbamoyladenosine(37)-C2) methyltransferase activity; IDA:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IDA: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; Q9BU70; HS. PE 1: Evidence at protein level; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1..441 FT /note="tRNA (adenine(37)-N6)-methyltransferase" FT /id="PRO_0000288886" FT DOMAIN 30..168 FT /note="TsaA-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01003" FT REGION 179..231 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 264..284 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 179..209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 210..231 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 VARIANT 7 FT /note="S -> P (in dbSNP:rs3183927)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_032527" FT VARIANT 252 FT /note="V -> A (in dbSNP:rs35606344)" FT /id="VAR_032528" FT VARIANT 324 FT /note="V -> M (in dbSNP:rs2282192)" FT /id="VAR_032529" FT CONFLICT 341 FT /note="F -> V (in Ref. 5; CAA60025)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="G -> D (in Ref. 1; BAA91013)" FT /evidence="ECO:0000305" SQ SEQUENCE 441 AA; 48587 MW; 84E6CF8BD294EDD2 CRC64; MRGLEESGPR PTATPCGCVK PALETGNLLT EPVGYLESCF SAKNGTPRQP SICSYSRACL RIRKRIFNNP EHSLMGLEQF SHVWILFVFH KNGHLSCKAK VQPPRLNGAK TGVFSTRSPH RPNAIGLTLA KLEKVEGGAI YLSGIDMIHG TPVLDIKPYI AEYDSPQNVM EPLADFNLQN NQHTPNTVSQ SDSKTDSCDQ RQLSGCDEPQ PHHSTKRKPK CPEDRTSEEN YLTHSDTARI QQAFPMHREI AVDFGLESRR DQSSSVAEEQ IGPYCPEKSF SEKGTDKKLE RVEGAAVLQG SRAETQPMAP HCPAGRADGA PRSVVPAWVT EAPVATLEVR FTPHAEMDLG QLSSQDVGQA SFKYFQSAEE AKRAIEAVLS ADPRSVYRRK LCQDRLFYFT VDIAHVTCWF GDGFAEVLRI KPASEPVHMT GPVGSLVSLG S //