TRMH_ECO57
ID TRMH_ECO57 Reviewed; 229 AA.
AC P0AGJ3; P19396;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=tRNA (guanosine(18)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_02060};
DE EC=2.1.1.34 {ECO:0000255|HAMAP-Rule:MF_02060};
DE AltName: Full=tRNA [Gm18] methyltransferase {ECO:0000255|HAMAP-Rule:MF_02060};
GN Name=trmH {ECO:0000255|HAMAP-Rule:MF_02060}; Synonyms=spoU;
GN OrderedLocusNames=Z5077, ECs4526;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in
CC tRNA. {ECO:0000255|HAMAP-Rule:MF_02060}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20077, Rhea:RHEA-COMP:10190, Rhea:RHEA-COMP:10192,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.34;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02060};
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000255|HAMAP-
CC Rule:MF_02060}.
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DR EMBL; AE005174; AAG58795.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37949.1; -; Genomic_DNA.
DR PIR; F91194; F91194.
DR PIR; G86041; G86041.
DR RefSeq; NP_312553.1; NC_002695.1.
DR RefSeq; WP_001070177.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AGJ3; -.
DR SMR; P0AGJ3; -.
DR STRING; 155864.EDL933_4914; -.
DR EnsemblBacteria; AAG58795; AAG58795; Z5077.
DR EnsemblBacteria; BAB37949; BAB37949; ECs_4526.
DR GeneID; 66672454; -.
DR GeneID; 915517; -.
DR KEGG; ece:Z5077; -.
DR KEGG; ecs:ECs_4526; -.
DR PATRIC; fig|386585.9.peg.4744; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_4_2_6; -.
DR OMA; TDRYQHV; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002938; P:tRNA guanine ribose methylation; IEA:UniProtKB-UniRule.
DR CDD; cd18092; SpoU-like_TrmH; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_02060; tRNA_methyltr_TrmH; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR022724; rRNA_MeTrfase_SpoU_C.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR033671; TrmH.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR43453; PTHR43453; 1.
DR Pfam; PF12105; SpoU_methylas_C; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..229
FT /note="tRNA (guanosine(18)-2'-O)-methyltransferase"
FT /id="PRO_0000159773"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
SQ SEQUENCE 229 AA; 25343 MW; BC5AB6B804BDEE2E CRC64;
MNPTRYARIC EMLARRQPDL TVCMEQVHKP HNVSAIIRTA DAVGVHEVHA VWPGSRMRTM
ASAAAGSNSW VQVKTHRTIG DAVAHLKGQG MQILATHLSD NAVDFREIDY TRPTCILMGQ
EKTGITQEAL ALADQDIIIP MIGMVQSLNV SVASALILYE AQRQRQNAGM YLRENSMLPE
AEQQRLLFEG GYPVLAKVAK RKGLPYPHVN QQGEIEADAD WWATMQAAG
