TRMH_THET2
ID TRMH_THET2 Reviewed; 194 AA.
AC Q72GI1;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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:7085632};
DE AltName: Full=tRNA [Gm18] methyltransferase {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000305};
GN Name=trmH {ECO:0000255|HAMAP-Rule:MF_02060};
GN OrderedLocusNames=TT_C1867 {ECO:0000312|EMBL:AAS82209.1};
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=7085632; DOI=10.1016/s0021-9258(18)34389-8;
RA Kumagai I., Watanabe K., Oshima T.;
RT "A thermostable tRNA (guanosine-2')-methyltransferase from Thermus
RT thermophilus HB27 and the effect of ribose methylation on the
RT conformational stability of tRNA.";
RL J. Biol. Chem. 257:7388-7395(1982).
CC -!- FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in
CC tRNA. {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000269|PubMed:7085632}.
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:7085632};
CC -!- ACTIVITY REGULATION: Stimulated by magnesium ions and spermine.
CC Inhibited by S-adenosyl-homocysteine. {ECO:0000269|PubMed:7085632}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:7085632};
CC KM=0.01 uM for E.coli tRNA(Phe) {ECO:0000269|PubMed:7085632};
CC Vmax=1.31 nmol/min/mg enzyme {ECO:0000269|PubMed:7085632};
CC pH dependence:
CC Optimum pH is 7.2-7.5. {ECO:0000269|PubMed:7085632};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7085632}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000255|HAMAP-
CC Rule:MF_02060, ECO:0000305}.
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DR EMBL; AE017221; AAS82209.1; -; Genomic_DNA.
DR RefSeq; WP_011174221.1; NC_005835.1.
DR AlphaFoldDB; Q72GI1; -.
DR SMR; Q72GI1; -.
DR STRING; 262724.TT_C1867; -.
DR EnsemblBacteria; AAS82209; AAS82209; TT_C1867.
DR GeneID; 3168939; -.
DR KEGG; tth:TT_C1867; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_4_2_0; -.
DR OMA; KIPMVGF; -.
DR OrthoDB; 1422015at2; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..194
FT /note="tRNA (guanosine(18)-2'-O)-methyltransferase"
FT /id="PRO_0000436161"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT BINDING 122..126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
SQ SEQUENCE 194 AA; 22084 MW; F499BB7E9AC1F5BF CRC64;
MRERTEARRR RIEEVLRRRQ PDLTVLLENV HKPHNLSAIL RTCDAVGVLE AHAVNPTGGV
PTFNETSGGS HKWVYLRVHP DLHEAFRFLK ERGFTVYATA LREDARDFRE VDYTKPTAVL
FGAEKWGVSE EALALADGAI KIPMLGMVQS LNVSVAAAVI LFEAQRQRLK AGLYDRPRLD
PELYQKVLAD WLRK
