TRMD_FUSNN
ID TRMD_FUSNN Reviewed; 238 AA.
AC Q8R5Y4;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=FN0283;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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}.
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DR EMBL; AE009951; AAL94489.1; -; Genomic_DNA.
DR RefSeq; NP_603190.1; NC_003454.1.
DR AlphaFoldDB; Q8R5Y4; -.
DR SMR; Q8R5Y4; -.
DR STRING; 190304.FN0283; -.
DR EnsemblBacteria; AAL94489; AAL94489; FN0283.
DR KEGG; fnu:FN0283; -.
DR PATRIC; fig|190304.8.peg.863; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_0; -.
DR InParanoid; Q8R5Y4; -.
DR OMA; ILCGHYK; -.
DR BioCyc; FNUC190304:G1FZS-881-MON; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
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..238
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060379"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 127..132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 238 AA; 27387 MW; 7A562AA005E3EBDD CRC64;
MKINILTLFP KMFDGFLSES IIARAIKFGA VEVNIIDIRD YCFDKHKQAD DMPFGGGNGM
VMKPEPLFLA LENVSGKVIY TSPQGKIFNQ EIAKELVKEE ELTIIAGHYE GVDERVVENK
VDMELSIGDF VLTGGEIAAM AISDTIIRLL PDVIKKESYE NDSFYNGLLD YPHYTRPAEY
KDLKVPEVLL SGNHKKIDEW RLKESLRRTY LRRRELIENR ELTKLEKKLL DEIKKEEV