ID   TRMI_THET8              Reviewed;         255 AA.
AC   Q5SKN4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase TrmI;
DE            EC=2.1.1.220;
DE   AltName: Full=tRNA(m1A58)-methyltransferase;
DE            Short=tRNA(m1A58)MTase;
GN   Name=trmI; OrderedLocusNames=TTHA0609;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of
CC       N(1)-methyladenine at position 58 (m1A58) in tRNA.
CC       {ECO:0000250|UniProtKB:Q8GBB2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00952};
CC   -!- SUBUNIT: Homotetramer composed of a dimer of dimers.
CC       {ECO:0000250|UniProtKB:Q8GBB2}.
CC   -!- DOMAIN: Contains a large catalytic C-terminal domain that binds S-
CC       adenosyl-L-methionine and a smaller N-terminal domain that may play a
CC       role in tRNA recognition. Domains are connected by a linker region.
CC       {ECO:0000250|UniProtKB:Q8GBB2}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR   EMBL; AP008226; BAD70432.1; -; Genomic_DNA.
DR   RefSeq; WP_011228067.1; NC_006461.1.
DR   RefSeq; YP_143875.1; NC_006461.1.
DR   AlphaFoldDB; Q5SKN4; -.
DR   SMR; Q5SKN4; -.
DR   STRING; 300852.55771991; -.
DR   EnsemblBacteria; BAD70432; BAD70432; BAD70432.
DR   GeneID; 3169400; -.
DR   KEGG; ttj:TTHA0609; -.
DR   PATRIC; fig|300852.9.peg.607; -.
DR   eggNOG; COG2519; Bacteria.
DR   HOGENOM; CLU_025402_0_1_0; -.
DR   OMA; VVYPKDA; -.
DR   PhylomeDB; Q5SKN4; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR   PANTHER; PTHR12133; PTHR12133; 1.
DR   Pfam; PF08704; GCD14; 1.
DR   PIRSF; PIRSF017269; GCD14; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51620; SAM_TRM61; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..255
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase TrmI"
FT                   /id="PRO_0000311813"
FT   BINDING         104..107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GBB2"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         155
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         170
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00952"
SQ   SEQUENCE   255 AA;  28568 MW;  0226E3502232BC5A CRC64;
     MAWPGPLLLK DRKGRAYLVF PKEGGVFHHH KGSVPHEALL EAGPGGVVRT HLGEELSVHR
     PTLEEYLLHM KRSATPTYPK DASAMVTLLD LAPGMRVLEA GTGSGGLTLF LARAVGEKGL
     VESYEARPHH LAQAERNVRA FWQVENVRFH LGKLEEAELE EAAYDGVALD LMEPWKALEK
     AALALKPDRF LVAYLPNITQ VLELVRAAEA HPFRLERVLE VGWREWEVRL PVAHPRFQQV
     GHTAFLVALR RWKAS