ID   TRMO_EIKCO              Reviewed;         176 AA.
AC   P37752;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=tRNA (adenine(37)-N6)-methyltransferase {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:P28634};
DE   AltName: Full=S-adenosylmethionine-dependent methyltransferase;
DE   AltName: Full=tRNA methyltransferase O {ECO:0000250|UniProtKB:P28634};
DE   Flags: Fragment;
GN   Name=trmO {ECO:0000250|UniProtKB:P28634};
OS   Eikenella corrodens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Eikenella.
OX   NCBI_TaxID=539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23834 / DSM 8340 / JCM 12952 / KCTC 15198 / LMG 15557 / NCTC
RC   10596 / 333/54-55;
RX   PubMed=8473871; DOI=10.1099/00221287-139-3-651;
RA   Rao V.K., Progulske-Fox A.;
RT   "Cloning and sequencing of two type 4 (N-methylphenylalanine) pilin genes
RT   from Eikenella corrodens.";
RL   J. Gen. Microbiol. 139:651-660(1993).
RN   [2]
RP   IDENTIFICATION.
RA   Rudd K.E., Koonin E.V.;
RL   Unpublished observations (APR-1994).
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(Thr)(GGU). The methyl group of
CC       m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA
CC       decoding ability. Binds to tRNA. {ECO:0000250|UniProtKB:P28634}.
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:P28634};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70028;
CC         Evidence={ECO:0000250|UniProtKB:P28634};
CC   -!- SIMILARITY: Belongs to the tRNA methyltransferase O family.
CC       {ECO:0000305}.
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DR   EMBL; Z12609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P37752; -.
DR   SMR; P37752; -.
DR   STRING; 539.A7P85_02425; -.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
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; IPR041369; TrmO_C.
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   Pfam; PF18389; TrmO_C; 1.
DR   SUPFAM; SSF118196; SSF118196; 1.
DR   TIGRFAMs; TIGR00104; tRNA_TsaA; 1.
DR   PROSITE; PS01318; TSAA_1; 1.
DR   PROSITE; PS51668; TSAA_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           <1..176
FT                   /note="tRNA (adenine(37)-N6)-methyltransferase"
FT                   /id="PRO_0000155618"
FT   DOMAIN          1..94
FT                   /note="TsaA-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01003"
FT   BINDING         12..13
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O29998"
FT   BINDING         12
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O29998"
FT   BINDING         50
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O29998"
FT   BINDING         74..77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O29998"
FT   NON_TER         1
SQ   SEQUENCE   176 AA;  19221 MW;  2B2984FCE7CC4D50 CRC64;
     SFSHIWVQFV FHGVAGAGWQ PLVRPPRLGG NRKMGVFATR SPFRPNPLGL SLLKLERIET
     EGGVRLWCGG ADLLDGTPVL DIKPYLPFVE AQPDAAPGFA AVPPVPLEVA WADEISAASL
     PPPNRLLIEQ SIAQDPRPAY QDTPQRVYKM AVDDWEVAFR IEKGMALIEA VMAVEG