TRMD_PSEAB
ID TRMD_PSEAB Reviewed; 252 AA.
AC Q02RL6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=PA14_15990;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ12977.1; -; Genomic_DNA.
DR RefSeq; WP_003137931.1; NZ_CP034244.1.
DR PDB; 5WYQ; X-ray; 2.16 A; A/B=5-250.
DR PDB; 5WYR; X-ray; 2.45 A; A/B=5-250.
DR PDBsum; 5WYQ; -.
DR PDBsum; 5WYR; -.
DR AlphaFoldDB; Q02RL6; -.
DR SMR; Q02RL6; -.
DR PRIDE; Q02RL6; -.
DR EnsemblBacteria; ABJ12977; ABJ12977; PA14_15990.
DR KEGG; pau:PA14_15990; -.
DR HOGENOM; CLU_047363_0_1_6; -.
DR OMA; ILCGHYK; -.
DR BioCyc; PAER208963:G1G74-1316-MON; -.
DR BRENDA; 2.1.1.228; 5087.
DR Proteomes; UP000000653; 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..252
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_1000072641"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 138..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5WYQ"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:5WYQ"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5WYR"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5WYQ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 206..224
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:5WYQ"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:5WYQ"
SQ SEQUENCE 252 AA; 28343 MW; 84796740210323F3 CRC64;
MDKRLWVGVV SIFPEMFRAI SDYGITSRAV KQGLLTLTCW NPRVYTEDRH QTVDDRPFGG
GPGMVMKIKP LEGALADARQ AAGGRKAKVI YLSPQGRQLT QAGVRELAEE EALILIAGRY
EGIDERFIEE HVDEEWSIGD YVLSGGELPA MVLVDAVTRL LPGALGHADS AEEDSFTDGL
LDCPHYTRPE VYADKRVPEV LLSGNHEHIR RWRLQQALGR TWERRADLLD SRSLSGEEQK
LLAEYIRQRD DS
