ID   TRMI_METJA              Reviewed;         282 AA.
AC   Q57598;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase TrmI;
DE            EC=2.1.1.219;
DE   AltName: Full=tRNA(m1A57/58)-methyltransferase;
GN   Name=trmI; OrderedLocusNames=MJ0134;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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(57)/adenosine(58) in tRNA + 2 S-adenosyl-L-
CC         methionine = 2 H(+) + N(1)-methyladenosine(57)/N(1)-
CC         methyladenosine(58) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:41740, Rhea:RHEA-COMP:9580, Rhea:RHEA-COMP:9582,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.219;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L77117; AAB98115.1; -; Genomic_DNA.
DR   PIR; F64316; F64316.
DR   RefSeq; WP_010869627.1; NC_000909.1.
DR   AlphaFoldDB; Q57598; -.
DR   SMR; Q57598; -.
DR   STRING; 243232.MJ_0134; -.
DR   EnsemblBacteria; AAB98115; AAB98115; MJ_0134.
DR   GeneID; 1450975; -.
DR   KEGG; mja:MJ_0134; -.
DR   eggNOG; arCOG00978; Archaea.
DR   HOGENOM; CLU_025402_0_1_2; -.
DR   InParanoid; Q57598; -.
DR   OMA; VVYPKDA; -.
DR   OrthoDB; 64860at2157; -.
DR   PhylomeDB; Q57598; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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..282
FT                   /note="tRNA (adenine(57)-N(1)/adenine(58)-N(1))-
FT                   methyltransferase TrmI"
FT                   /id="PRO_0000106712"
FT   BINDING         98..101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GBB2"
FT   BINDING         119
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00952"
SQ   SEQUENCE   282 AA;  32207 MW;  558FB972B21CFA9C CRC64;
     MFAYKLLVDE RGKRYLLKKN VEKFGTDLGI VDMKDIEEGV ELKSHKGHTF YLVEPTMFDI
     LKRMKRTVTT LLPKDIGFII ARAGIREGET VVEAGTGSGA LTMYLSNAVG KTGKVITYDI
     RPEFAKVARK NLLRVGAIKK GQKIIGLDEE FDDEDEIEIE DGLFNVIQKI GDVREKIDEK
     DVDVIVLDLP DPWNVVENAK KALNKKRGRI VTYLPYIEQV KKTVEKLKEE GFWDIHTYEI
     IEREIEISEK GVRPSTRMIG HTGYITVARV PPEPLDREEE KE