TRMH_SHIFL
ID TRMH_SHIFL Reviewed; 229 AA.
AC P0AGJ4; P19396;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SF3691, S4078;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45138.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19055.1; -; Genomic_DNA.
DR RefSeq; NP_709431.1; NC_004337.2.
DR RefSeq; WP_001070177.1; NZ_WPGW01000042.1.
DR AlphaFoldDB; P0AGJ4; -.
DR SMR; P0AGJ4; -.
DR STRING; 198214.SF3691; -.
DR PRIDE; P0AGJ4; -.
DR EnsemblBacteria; AAN45138; AAN45138; SF3691.
DR EnsemblBacteria; AAP19055; AAP19055; S4078.
DR GeneID; 1026190; -.
DR GeneID; 66672454; -.
DR KEGG; sfl:SF3691; -.
DR KEGG; sfx:S4078; -.
DR PATRIC; fig|198214.7.peg.4355; -.
DR HOGENOM; CLU_021322_4_2_6; -.
DR OMA; TDRYQHV; -.
DR OrthoDB; 1422015at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000159774"
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
