TRMO_RAT
ID TRMO_RAT Reviewed; 431 AA.
AC Q4V7E0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=tRNA (adenine(37)-N6)-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9BU70};
DE AltName: Full=tRNA methyltransferase O {ECO:0000312|RGD:1305420};
GN Name=Trmo {ECO:0000312|RGD:1305420};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 -!- SIMILARITY: Belongs to the tRNA methyltransferase O family.
CC {ECO:0000305}.
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DR EMBL; BC097981; AAH97981.1; -; mRNA.
DR RefSeq; NP_001020823.1; NM_001025652.1.
DR AlphaFoldDB; Q4V7E0; -.
DR SMR; Q4V7E0; -.
DR STRING; 10116.ENSRNOP00000012602; -.
DR PaxDb; Q4V7E0; -.
DR PRIDE; Q4V7E0; -.
DR Ensembl; ENSRNOT00000012602; ENSRNOP00000012602; ENSRNOG00000009492.
DR GeneID; 298072; -.
DR KEGG; rno:298072; -.
DR UCSC; RGD:1305420; rat.
DR CTD; 51531; -.
DR RGD; 1305420; Trmo.
DR eggNOG; KOG2942; Eukaryota.
DR GeneTree; ENSGT00390000004643; -.
DR HOGENOM; CLU_013458_1_0_1; -.
DR InParanoid; Q4V7E0; -.
DR OMA; YRRKHCQ; -.
DR OrthoDB; 1483097at2759; -.
DR PhylomeDB; Q4V7E0; -.
DR PRO; PR:Q4V7E0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009492; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q4V7E0; RN.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016430; F:tRNA (adenine-N6-)-methyltransferase activity; ISO:RGD.
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 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_0000288888"
FT DOMAIN 30..168
FT /note="TsaA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01003"
FT REGION 167..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..243
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"
SQ SEQUENCE 431 AA; 47595 MW; 05D283EAAF82F316 CRC64;
MRGLEKQGPS ATAAPCGCAQ PALETGNLLT EPIGYLESCF SAKIGTPRQP SICSQSRACL
KIRKSIFNNP EHSLMGLEQF SHVWILFVFH KNGHLNYKAK VQPPRLNGAK TGVFSTRSPH
RPNAIGLTLA KLEKVEGGAV YLSGIDMIHG TPVLDIKPYI ADYDSPQNLE PQTKHHKLRA
AGPSDATANS CDQQLLSGCE KAQPCHSTKE KPKCREHRTS DENSQKFRDT SEIQHTLPED
RERAVDLALE SSREETMDEP EDQLGPQELK SFLEEGTDRP RKVEGALVLR GSSAETRWDA
SCHARTADRV PCSVVPSWVK EAPVATLQVR FTPHAEMDLR KLSSGGASQT SFKYFHSAEE
AKCAIEAMLS ADPRSVYRRK LCEDRLFFFT VDIAHVTCWF GDGFAEVLRI KLASEPVEVA
DPEESLVALG S
