TRMH_AQUAE
ID TRMH_AQUAE Reviewed; 211 AA.
AC O67577;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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:12704200};
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:12704200};
GN Synonyms=spoU {ECO:0000303|PubMed:12704200}; OrderedLocusNames=aq_1661;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12704200; DOI=10.1074/jbc.m212577200;
RA Hori H., Kubota S., Watanabe K., Kim J.M., Ogasawara T., Sawasaki T.,
RA Endo Y.;
RT "Aquifex aeolicus tRNA (Gm18) methyltransferase has unique substrate
RT specificity. TRNA recognition mechanism of the enzyme.";
RL J. Biol. Chem. 278:25081-25090(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND SUBUNIT.
RX PubMed=16511140; DOI=10.1107/s1744309105022980;
RA Pleshe E., Truesdell J., Batey R.T.;
RT "Structure of a class II TrmH tRNA-modifying enzyme from Aquifex
RT aeolicus.";
RL Acta Crystallogr. F 61:722-728(2005).
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:12704200}.
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:12704200};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16511140}.
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; AE000657; AAC07528.1; -; Genomic_DNA.
DR PIR; H70443; H70443.
DR RefSeq; NP_214143.1; NC_000918.1.
DR RefSeq; WP_010881080.1; NC_000918.1.
DR PDB; 1ZJR; X-ray; 1.85 A; A=1-211.
DR PDBsum; 1ZJR; -.
DR AlphaFoldDB; O67577; -.
DR SMR; O67577; -.
DR STRING; 224324.aq_1661; -.
DR PRIDE; O67577; -.
DR EnsemblBacteria; AAC07528; AAC07528; aq_1661.
DR KEGG; aae:aq_1661; -.
DR PATRIC; fig|224324.8.peg.1283; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_4_2_0; -.
DR InParanoid; O67577; -.
DR OMA; KIPMVGF; -.
DR OrthoDB; 1422015at2; -.
DR BRENDA; 2.1.1.34; 396.
DR EvolutionaryTrace; O67577; -.
DR Proteomes; UP000000798; 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 3D-structure; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..211
FT /note="tRNA (guanosine(18)-2'-O)-methyltransferase"
FT /id="PRO_0000159771"
FT BINDING 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT BINDING 155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:1ZJR"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:1ZJR"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1ZJR"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:1ZJR"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1ZJR"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1ZJR"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1ZJR"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 157..174
FT /evidence="ECO:0007829|PDB:1ZJR"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1ZJR"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:1ZJR"
SQ SEQUENCE 211 AA; 24488 MW; D68A015C7464491A CRC64;
MVMEYLVLEK RLKRLREVLE KRQKDLIVFA DNVKNEHNFS AIVRTCDAVG VLYLYYYHAE
GKKAKINEGI TQGSHKWVFI EKVDNPVQKL LEFKNRGFQI VATWLSKESV NFREVDYTKP
TVLVVGNELQ GVSPEIVEIA DKKIVIPMYG MAQSLNVSVA TGIILYEAQR QREEKGMYSR
PSLSEEEIQK ILKKWAYEDV IKERKRTLST S
