TRMD_PSEAE
ID TRMD_PSEAE Reviewed; 252 AA.
AC Q9HXQ1;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=PA3743;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG07130.1; -; Genomic_DNA.
DR PIR; C83178; C83178.
DR RefSeq; NP_252432.1; NC_002516.2.
DR RefSeq; WP_003119312.1; NZ_QZGE01000001.1.
DR PDB; 5ZHM; X-ray; 2.76 A; A/B=5-250.
DR PDB; 5ZHN; X-ray; 2.65 A; A/B=5-250.
DR PDB; 6AFK; X-ray; 2.75 A; A/B=5-250.
DR PDB; 6JKI; X-ray; 2.59 A; A/B=5-252.
DR PDB; 6JOE; X-ray; 2.21 A; A/B=5-250.
DR PDBsum; 5ZHM; -.
DR PDBsum; 5ZHN; -.
DR PDBsum; 6AFK; -.
DR PDBsum; 6JKI; -.
DR PDBsum; 6JOE; -.
DR AlphaFoldDB; Q9HXQ1; -.
DR SMR; Q9HXQ1; -.
DR STRING; 287.DR97_4133; -.
DR BindingDB; Q9HXQ1; -.
DR ChEMBL; CHEMBL4523932; -.
DR PaxDb; Q9HXQ1; -.
DR PRIDE; Q9HXQ1; -.
DR EnsemblBacteria; AAG07130; AAG07130; PA3743.
DR GeneID; 880357; -.
DR KEGG; pae:PA3743; -.
DR PATRIC; fig|208964.12.peg.3915; -.
DR PseudoCAP; PA3743; -.
DR HOGENOM; CLU_047363_0_1_6; -.
DR InParanoid; Q9HXQ1; -.
DR OMA; ILCGHYK; -.
DR PhylomeDB; Q9HXQ1; -.
DR BioCyc; PAER208964:G1FZ6-3814-MON; -.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..252
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060433"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 138..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:6JKI"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:6JKI"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6JKI"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:6JKI"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:6JKI"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:6JKI"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6JKI"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 206..224
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:6JKI"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:6JKI"
SQ SEQUENCE 252 AA; 28359 MW; 8875B993DF0FF00D CRC64;
MDKRLWVGVV SIFPEMFRAI SDYGITSRAV KQGLLTLTCW NPRDYTEDRH QTVDDRPFGG
GPGMVMKIKP LEGALADARQ AAGGRKAKVI YLSPQGRQLT QAGVRELAEE EALILIAGRY
EGIDERFIEE HVDEEWSIGD YVLSGGELPA MVLVDAVTRL LPGALGHADS AEEDSFTDGL
LDCPHYTRPE VYADKRVPEV LLSGNHEHIR RWRLQQALGR TWERRADLLD SRSLSGEEQK
LLAEYIRQRD DS
