TRMD_CORDI
ID TRMD_CORDI Reviewed; 292 AA.
AC Q6NGI5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-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=DIP1530;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248358; CAE50056.1; -; Genomic_DNA.
DR RefSeq; WP_010935129.1; NC_002935.2.
DR PDB; 7KFF; X-ray; 1.35 A; A=1-292.
DR PDBsum; 7KFF; -.
DR AlphaFoldDB; Q6NGI5; -.
DR SMR; Q6NGI5; -.
DR STRING; 257309.DIP1530; -.
DR EnsemblBacteria; CAE50056; CAE50056; DIP1530.
DR KEGG; cdi:DIP1530; -.
DR HOGENOM; CLU_047363_0_0_11; -.
DR OMA; ILCGHYK; -.
DR OrthoDB; 525632at2; -.
DR Proteomes; UP000002198; 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; -; 2.
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; 2.
DR Pfam; PF01746; tRNA_m1G_MT; 2.
DR PIRSF; PIRSF000386; tRNA_mtase; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..292
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060363"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 175..180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:7KFF"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:7KFF"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:7KFF"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:7KFF"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:7KFF"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:7KFF"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:7KFF"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:7KFF"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:7KFF"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:7KFF"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:7KFF"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:7KFF"
SQ SEQUENCE 292 AA; 32418 MW; 4B6ABDD03F1D1A09 CRC64;
MRLDVITIFP EYLDPLRHAL LGKAIEKDLL SVGVHDLRLW AEDAHKSVDD SPFGGGPGMV
MKPTVWGPAL DDVATMSGKA HMGAQLDSAR VHVDKPRHDE LEGIQFAGYD AAEVAEADKP
LLLVPTPAGA PFTQEDARAW SNEEHIVFAC GRYEGIDQRV IEDAKKTYRV REVSIGDYVL
IGGEVAVLVI AEAVVRLIPG VLGNTQSHQD DSFSDGLLEG PSYTKPREWR GLEVPEVLTS
GNHAKIERWR REQSLKRTWE VRPELLDGME LDRHDQAYVE GLRRGNTSDN LN
