TRMD_META1
ID TRMD_META1 Reviewed; 228 AA.
AC B3PMA2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
GN OrderedLocusNames=MARTH_orf246;
OS Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=243272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=158L3-1;
RX PubMed=18573899; DOI=10.1128/iai.00516-08;
RA Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA Loraine A.E.;
RT "Genome of Mycoplasma arthritidis.";
RL Infect. Immun. 76:4000-4008(2008).
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; CP001047; ACF07154.1; -; Genomic_DNA.
DR RefSeq; WP_012498111.1; NC_011025.1.
DR AlphaFoldDB; B3PMA2; -.
DR SMR; B3PMA2; -.
DR STRING; 243272.MARTH_orf246; -.
DR EnsemblBacteria; ACF07154; ACF07154; MARTH_orf246.
DR KEGG; mat:MARTH_orf246; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_14; -.
DR OMA; ILCGHYK; -.
DR OrthoDB; 525632at2; -.
DR Proteomes; UP000008812; 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..228
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_1000130188"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 127..132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
SQ SEQUENCE 228 AA; 25752 MW; D6A27C1E3E4E14A2 CRC64;
MKINILSLFP EYFKAFQENS MIAKAIKLGH LEINVINFRD FSKEKHQKVD DTVYGGGDGM
LLQVEPIDLA LESVPNSYKI LLSPQGQVFN QTKAHELAKH QEITLVCGHY EGFDERVLEF
VDEELSVGDF ILTGGEIPAM LITEAVARLV PGVLKKGSHE NESFEGDGLL DYPQYTKPAI
YKGLKVPEVL LSGNHALIDR WRKEASYSKT LKNRKDILAK RKEKPHEN
