TRMH_ECOLI
ID TRMH_ECOLI Reviewed; 229 AA.
AC P0AGJ2; P19396; Q2M7W4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=tRNA (guanosine(18)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000305};
DE EC=2.1.1.34 {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000269|PubMed:9321663};
DE AltName: Full=tRNA [Gm18] methyltransferase {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000305};
GN Name=trmH {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000303|PubMed:9321663};
GN Synonyms=spoU {ECO:0000303|PubMed:2005134};
GN OrderedLocusNames=b3651, JW3626;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=2549050; DOI=10.1016/s0021-9258(18)63813-x;
RA Sarubbi E., Rudd K.E., Xiao H., Ikehara K., Kalman M., Cashel M.;
RT "Characterization of the spoT gene of Escherichia coli.";
RL J. Biol. Chem. 264:15074-15082(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP GENE NAME.
RX PubMed=2005134; DOI=10.1016/s0021-9258(19)67694-5;
RA Xiao H., Kalman M., Ikehara K., Zemel S., Glaser G., Cashel M.;
RT "Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null
RT mutants can be eliminated by spoT null mutations.";
RL J. Biol. Chem. 266:5980-5990(1991).
RN [6]
RP POSSIBLE FUNCTION.
RX PubMed=8265370; DOI=10.1093/nar/21.23.5519;
RA Koonin E.V., Rudd K.E.;
RT "SpoU protein of Escherichia coli belongs to a new family of putative rRNA
RT methylases.";
RL Nucleic Acids Res. 21:5519-5519(1993).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9321663; DOI=10.1093/nar/25.20.4093;
RA Persson B.C., Jaeger G., Gustafsson C.;
RT "The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is
RT essential for tRNA (Gm18) 2'-O-methyltransferase activity.";
RL Nucleic Acids Res. 25:4093-4097(1997).
CC -!- FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in
CC tRNA. Type II methylase, which methylates only a subset of tRNA
CC species. {ECO:0000269|PubMed:9321663}.
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 ECO:0000269|PubMed:9321663};
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; M24503; AAB00161.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62004.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76675.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77642.1; -; Genomic_DNA.
DR PIR; JV0043; JV0043.
DR RefSeq; NP_418108.1; NC_000913.3.
DR RefSeq; WP_001070177.1; NZ_STEB01000024.1.
DR AlphaFoldDB; P0AGJ2; -.
DR SMR; P0AGJ2; -.
DR BioGRID; 4262569; 162.
DR BioGRID; 852468; 7.
DR DIP; DIP-35977N; -.
DR IntAct; P0AGJ2; 11.
DR STRING; 511145.b3651; -.
DR jPOST; P0AGJ2; -.
DR PaxDb; P0AGJ2; -.
DR PRIDE; P0AGJ2; -.
DR EnsemblBacteria; AAC76675; AAC76675; b3651.
DR EnsemblBacteria; BAE77642; BAE77642; BAE77642.
DR GeneID; 66672454; -.
DR GeneID; 948161; -.
DR KEGG; ecj:JW3626; -.
DR KEGG; eco:b3651; -.
DR PATRIC; fig|1411691.4.peg.3055; -.
DR EchoBASE; EB0960; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_4_2_6; -.
DR InParanoid; P0AGJ2; -.
DR OMA; TDRYQHV; -.
DR PhylomeDB; P0AGJ2; -.
DR BioCyc; EcoCyc:EG10967-MON; -.
DR BioCyc; MetaCyc:EG10967-MON; -.
DR PRO; PR:P0AGJ2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
DR GO; GO:0030488; P:tRNA methylation; TAS:EcoliWiki.
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 1: Evidence at protein level;
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_0000159772"
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
