TRMD_BARHE
ID TRMD_BARHE Reviewed; 232 AA.
AC Q6G1R9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=BH15820;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF28345.1; -; Genomic_DNA.
DR RefSeq; WP_011181348.1; NZ_LRIJ02000001.1.
DR PDB; 3IEF; X-ray; 2.50 A; A/B=1-232.
DR PDBsum; 3IEF; -.
DR AlphaFoldDB; Q6G1R9; -.
DR SMR; Q6G1R9; -.
DR STRING; 283166.BH15820; -.
DR PaxDb; Q6G1R9; -.
DR PRIDE; Q6G1R9; -.
DR EnsemblBacteria; CAF28345; CAF28345; BH15820.
DR GeneID; 64157720; -.
DR KEGG; bhe:BH15820; -.
DR eggNOG; COG0336; Bacteria.
DR OMA; ILCGHYK; -.
DR EvolutionaryTrace; Q6G1R9; -.
DR Proteomes; UP000000421; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..232
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060331"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 131..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:3IEF"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:3IEF"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3IEF"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:3IEF"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:3IEF"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3IEF"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3IEF"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 199..217
FT /evidence="ECO:0007829|PDB:3IEF"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:3IEF"
SQ SEQUENCE 232 AA; 25463 MW; 4C89D122DB57C9BB CRC64;
MKFQARVLTL YPEMFPGFLG CSLAGQALKQ GIWSLETVQI RDFALDKHHS VDDTPAGGGA
GMVMRADVLA AALDSCPNDS PRLLMSPRGR LLNQAYARSL ARSSGVTLVC GRFEGVDERI
IEARELEEVS IGDYILSGGE TAALVLLDAI VRLLPGVMGN EISAKCESFE NGLLEHPQYT
RPAVFEGRGI PPVLTSGHHK AIANWRQQQA ESLTRQRRPD LYALYNKNRQ KT
