TRMD_ACIBY
ID TRMD_ACIBY Reviewed; 246 AA.
AC B0V8J1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=ABAYE0323;
OS Acinetobacter baumannii (strain AYE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509173;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYE;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU459141; CAM85301.1; -; Genomic_DNA.
DR RefSeq; WP_000464595.1; NC_010410.1.
DR PDB; 7MYQ; X-ray; 2.55 A; A/B=2-246.
DR PDB; 7MYS; X-ray; 2.40 A; A/B=2-246.
DR PDBsum; 7MYQ; -.
DR PDBsum; 7MYS; -.
DR AlphaFoldDB; B0V8J1; -.
DR SMR; B0V8J1; -.
DR EnsemblBacteria; CAM85301; CAM85301; ABAYE0323.
DR KEGG; aby:ABAYE0323; -.
DR HOGENOM; CLU_047363_0_1_6; -.
DR OMA; ILCGHYK; -.
DR Proteomes; UP000002446; 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..246
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_1000130123"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 137..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:7MYS"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:7MYS"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:7MYS"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:7MYS"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:7MYS"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:7MYS"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:7MYS"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:7MYS"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 205..223
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:7MYS"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:7MYS"
SQ SEQUENCE 246 AA; 27895 MW; FC3A78302FED3E4C CRC64;
MFFAVITLFP EMFDAITAYG ISGRAAKRDI VQVTCINPRD FAEGNYRRVD ERPFGGGPGM
VMMAEPLAKA INHAKQLASR AGCVHVPVVY MSPQGKTLNE QAVQQFVDYD GLIVLCGRYE
GVDERLIQHY VDQEWSIGDY VLSGGELPAM VLLDSIIRRL PNVMSDEQSA IQDSFVDGLL
DCPQYTKPDQ FEGLDVPEIL KSGHHANIEK WRFLQRYQRT LERRPELIEQ VTLTKQQKKW
LSDEQG
