ID   TRMI_MYCTO              Reviewed;         280 AA.
AC   P9WFZ0; L0TA90; O33253; Q7D7H7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
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=MT2178;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK46461.1; -; Genomic_DNA.
DR   PIR; A70513; A70513.
DR   RefSeq; WP_003411041.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFZ0; -.
DR   SMR; P9WFZ0; -.
DR   EnsemblBacteria; AAK46461; AAK46461; MT2178.
DR   GeneID; 45426093; -.
DR   KEGG; mtc:MT2178; -.
DR   PATRIC; fig|83331.31.peg.2348; -.
DR   HOGENOM; CLU_025402_0_0_11; -.
DR   Proteomes; UP000001020; 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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..280
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase TrmI"
FT                   /id="PRO_0000428453"
FT   BINDING         110..113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFZ1"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFZ1,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFZ1,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFZ1,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         178
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFZ1,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
SQ   SEQUENCE   280 AA;  30123 MW;  D09F0CEFC6778935 CRC64;
     MSATGPFSIG ERVQLTDAKG RRYTMSLTPG AEFHTHRGSI AHDAVIGLEQ GSVVKSSNGA
     LFLVLRPLLV DYVMSMPRGP QVIYPKDAAQ IVHEGDIFPG ARVLEAGAGS GALTLSLLRA
     VGPAGQVISY EQRADHAEHA RRNVSGCYGQ PPDNWRLVVS DLADSELPDG SVDRAVLDML
     APWEVLDAVS RLLVAGGVLM VYVATVTQLS RIVEALRAKQ CWTEPRAWET LQRGWNVVGL
     AVRPQHSMRG HTAFLVATRR LAPGAVAPAP LGRKREGRDG