TRMO_HUMAN
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 03-AUG-2022, entry version 136.
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};
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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; Q9BU70; -.
DR PeptideAtlas; Q9BU70; -.
DR PRIDE; Q9BU70; -.
DR ProteomicsDB; 79058; -.
DR Antibodypedia; 28898; 168 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 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; YRRKHCQ; -.
DR OrthoDB; 1483097at2759; -.
DR PhylomeDB; Q9BU70; -.
DR TreeFam; TF331670; -.
DR PathwayCommons; Q9BU70; -.
DR SignaLink; Q9BU70; -.
DR BioGRID-ORCS; 51531; 12 hits in 1060 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 177 other tissues.
DR ExpressionAtlas; Q9BU70; baseline and differential.
DR Genevisible; Q9BU70; HS.
DR GO; GO:0089715; F:tRNA m6t6A37 methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA: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 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
