TRMD_HAEIN
ID TRMD_HAEIN Reviewed; 246 AA.
AC P43912;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=HI_0202;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RX PubMed=12773376; DOI=10.1093/emboj/cdg269;
RA Ahn H.J., Kim H.-W., Yoon H.-J., Lee B.I., Suh S.W., Yang J.K.;
RT "Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA
RT recognition.";
RL EMBO J. 22:2593-2603(2003).
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:0000269|PubMed:12773376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC21871.1; -; Genomic_DNA.
DR PIR; C64054; C64054.
DR RefSeq; NP_438371.1; NC_000907.1.
DR RefSeq; WP_005661387.1; NC_000907.1.
DR PDB; 1UAJ; X-ray; 1.85 A; A=1-246.
DR PDB; 1UAK; X-ray; 2.05 A; A=1-246.
DR PDB; 1UAL; X-ray; 1.80 A; A=1-246.
DR PDB; 1UAM; X-ray; 2.20 A; A=1-246.
DR PDB; 3AXZ; X-ray; 2.25 A; A=1-246.
DR PDB; 4MCB; X-ray; 1.94 A; A/B=1-246.
DR PDB; 4MCC; X-ray; 1.95 A; A/B=1-246.
DR PDB; 4MCD; X-ray; 1.55 A; A=1-246.
DR PDB; 4YPW; X-ray; 2.31 A; A=1-246.
DR PDB; 4YPX; X-ray; 1.89 A; A=1-246.
DR PDB; 4YPY; X-ray; 1.90 A; A=1-246.
DR PDB; 4YPZ; X-ray; 1.84 A; A=1-246.
DR PDB; 4YQ0; X-ray; 1.76 A; A=1-246.
DR PDB; 4YQ1; X-ray; 2.00 A; A=1-246.
DR PDB; 4YQ2; X-ray; 2.65 A; A=1-246.
DR PDB; 4YQ3; X-ray; 2.49 A; A=1-246.
DR PDB; 4YQ4; X-ray; 1.89 A; A=1-246.
DR PDB; 4YQ5; X-ray; 1.76 A; A=1-246.
DR PDB; 4YQ6; X-ray; 1.90 A; A=1-246.
DR PDB; 4YQ7; X-ray; 1.80 A; A=1-246.
DR PDB; 4YQ8; X-ray; 1.94 A; A=1-246.
DR PDB; 4YQ9; X-ray; 1.64 A; A=1-246.
DR PDB; 4YQA; X-ray; 1.55 A; A=1-246.
DR PDB; 4YQB; X-ray; 2.10 A; A=1-246.
DR PDB; 4YQC; X-ray; 1.89 A; A=1-246.
DR PDB; 4YQD; X-ray; 1.45 A; A=1-246.
DR PDB; 4YQG; X-ray; 1.86 A; A=1-246.
DR PDB; 4YQI; X-ray; 1.92 A; A=1-246.
DR PDB; 4YQJ; X-ray; 1.94 A; A=1-246.
DR PDB; 4YQK; X-ray; 1.83 A; A=1-246.
DR PDB; 4YQL; X-ray; 2.40 A; A=1-246.
DR PDB; 4YQN; X-ray; 2.20 A; A=1-246.
DR PDB; 4YQO; X-ray; 1.68 A; A=1-246.
DR PDB; 4YQP; X-ray; 2.60 A; A=1-246.
DR PDB; 4YQQ; X-ray; 1.78 A; A=1-246.
DR PDB; 4YQR; X-ray; 1.70 A; A=1-246.
DR PDB; 4YQS; X-ray; 1.90 A; A=1-246.
DR PDB; 4YQT; X-ray; 1.60 A; A=1-246.
DR PDB; 4YVG; X-ray; 1.55 A; A=1-246.
DR PDB; 4YVH; X-ray; 1.60 A; A=1-246.
DR PDB; 4YVI; X-ray; 3.01 A; A/B=1-246.
DR PDB; 4YVJ; X-ray; 2.90 A; A/B=1-246.
DR PDB; 4YVK; X-ray; 3.00 A; A/B=1-246.
DR PDB; 5D9F; X-ray; 1.91 A; A=1-246.
DR PDBsum; 1UAJ; -.
DR PDBsum; 1UAK; -.
DR PDBsum; 1UAL; -.
DR PDBsum; 1UAM; -.
DR PDBsum; 3AXZ; -.
DR PDBsum; 4MCB; -.
DR PDBsum; 4MCC; -.
DR PDBsum; 4MCD; -.
DR PDBsum; 4YPW; -.
DR PDBsum; 4YPX; -.
DR PDBsum; 4YPY; -.
DR PDBsum; 4YPZ; -.
DR PDBsum; 4YQ0; -.
DR PDBsum; 4YQ1; -.
DR PDBsum; 4YQ2; -.
DR PDBsum; 4YQ3; -.
DR PDBsum; 4YQ4; -.
DR PDBsum; 4YQ5; -.
DR PDBsum; 4YQ6; -.
DR PDBsum; 4YQ7; -.
DR PDBsum; 4YQ8; -.
DR PDBsum; 4YQ9; -.
DR PDBsum; 4YQA; -.
DR PDBsum; 4YQB; -.
DR PDBsum; 4YQC; -.
DR PDBsum; 4YQD; -.
DR PDBsum; 4YQG; -.
DR PDBsum; 4YQI; -.
DR PDBsum; 4YQJ; -.
DR PDBsum; 4YQK; -.
DR PDBsum; 4YQL; -.
DR PDBsum; 4YQN; -.
DR PDBsum; 4YQO; -.
DR PDBsum; 4YQP; -.
DR PDBsum; 4YQQ; -.
DR PDBsum; 4YQR; -.
DR PDBsum; 4YQS; -.
DR PDBsum; 4YQT; -.
DR PDBsum; 4YVG; -.
DR PDBsum; 4YVH; -.
DR PDBsum; 4YVI; -.
DR PDBsum; 4YVJ; -.
DR PDBsum; 4YVK; -.
DR PDBsum; 5D9F; -.
DR AlphaFoldDB; P43912; -.
DR SMR; P43912; -.
DR STRING; 71421.HI_0202; -.
DR BindingDB; P43912; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR EnsemblBacteria; AAC21871; AAC21871; HI_0202.
DR KEGG; hin:HI_0202; -.
DR PATRIC; fig|71421.8.peg.207; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_6; -.
DR OMA; ILCGHYK; -.
DR PhylomeDB; P43912; -.
DR BioCyc; HINF71421:G1GJ1-213-MON; -.
DR BRENDA; 2.1.1.228; 2529.
DR EvolutionaryTrace; P43912; -.
DR Proteomes; UP000000579; 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..246
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060385"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 133..138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:4YQD"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:4YQD"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4YQD"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:4YQD"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:4YQD"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:4YQD"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4YVH"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:4YQD"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4YVJ"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:4YVG"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4YVG"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 201..219
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:4YQD"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:4YQD"
SQ SEQUENCE 246 AA; 27543 MW; DEEF238159B1003D CRC64;
MWIGVISLFP EMFKAITEFG VTGRAVKHNL LKVECWNPRD FTFDKHKTVD DRPYGGGPGM
LMMVQPLRDA IHTAKAAAGE GAKVIYLSPQ GRKLDQGGVT ELAQNQKLIL VCGRYEGIDE
RLIQTEIDEE WSIGDYVLTG GELPAMTLID AVARFIPGVL GKQASAEEDS FADGLLDCPH
YTRPEVLEGL TVPPVLMSGH HEEIRKWRLK QSLQRTWLRR PELLEGLALT DEQRKLLKEA
QAEHNS
