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TRMD_LACLA
ID   TRMD_LACLA              Reviewed;         247 AA.
AC   Q9CFB7;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase;
DE            EC=2.1.1.228;
DE   AltName: Full=M1G-methyltransferase;
DE   AltName: Full=tRNA [GM37] methyltransferase;
GN   Name=trmD; OrderedLocusNames=LL1564; ORFNames=L6128;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK05662.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005176; AAK05662.1; ALT_INIT; Genomic_DNA.
DR   PIR; D86820; D86820.
DR   RefSeq; NP_267720.2; NC_002662.1.
DR   RefSeq; WP_003130706.1; NC_002662.1.
DR   AlphaFoldDB; Q9CFB7; -.
DR   SMR; Q9CFB7; -.
DR   STRING; 272623.L6128; -.
DR   PaxDb; Q9CFB7; -.
DR   EnsemblBacteria; AAK05662; AAK05662; L6128.
DR   KEGG; lla:L6128; -.
DR   PATRIC; fig|272623.7.peg.1682; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_1_9; -.
DR   OMA; ILCGHYK; -.
DR   Proteomes; UP000002196; 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; 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   PIRSF; PIRSF000386; tRNA_mtase; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00088; trmD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..247
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000060394"
FT   BINDING         112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         131..136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   247 AA;  28245 MW;  7B79B009B3896126 CRC64;
     MRIDILSIFP EMFGPLNQSI VGKAQDKGIL ELHTHDFREN ATNKQRHVDD MPYGGGQGML
     LMPQPIFDTM DKIPQKPEKP ARVILLDPAG KKFDQKMAEE LSQEEQLIFI CGHYEGYDER
     IKTLVTDEIS LGDFVLTGGE VAATVMVDAV VRLIPGVLGK VASHEDDSFS SGLLEYPQYT
     RPEDFRGMKV PEVLMSGHHE NIRKWRLKES LRKTLERRPD LLDKYEPNEE ELKMLQLLRE
     NVQDVVE
 
 
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