ID   TRMD_CHLAB              Reviewed;         355 AA.
AC   Q5L5L8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE            EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_00605};
DE   AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
GN   Name=trmD {ECO:0000255|HAMAP-Rule:MF_00605}; OrderedLocusNames=CAB627;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00605};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000255|HAMAP-Rule:MF_00605}.
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DR   EMBL; CR848038; CAH64073.1; -; Genomic_DNA.
DR   RefSeq; WP_011097214.1; NC_004552.2.
DR   AlphaFoldDB; Q5L5L8; -.
DR   SMR; Q5L5L8; -.
DR   EnsemblBacteria; CAH64073; CAH64073; CAB627.
DR   KEGG; cab:CAB627; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_2_0; -.
DR   OMA; ILCGHYK; -.
DR   OrthoDB; 525632at2; -.
DR   Proteomes; UP000001012; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd18080; TrmD-like; 1.
DR   Gene3D; 1.10.1270.20; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_bac.
DR   InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR46417; PTHR46417; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00088; trmD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..355
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000060356"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT   BINDING         129..134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
SQ   SEQUENCE   355 AA;  40633 MW;  0A0840F2ABDA7EC5 CRC64;
     MKIDILSLFP EYFDSPLRSS ILGRAIKRGL LDIQSRDIRE FGLGKWKQVD DAPFNHDGML
     LMAEPVVKAI RHVKRSDSKV VYLSPQGQLL TAKKSRELAQ CSHLIFLCGH YEGIDERALE
     SEVDEEISIG DYVLTNGGIA ALVVIDALSR FIPGVLGNQE SADKDSMENG LLEGPQYTRP
     RVFEGREVPE VLLHGDHQAI AKWRKQISLD RTRERRPDLY IRYLYDRENE EVTQQETDLK
     QSMLEGESAV ILEVEDLHRS RKFYSKMFRL NQPVNNRLHI PGKTQMTIHL QEVGLKSKNI
     VLLSLRLGCK DDFFSFLGRW KMLGGTLEQA DDRGEVRLVR DFDGHVWAIS CKQAE