ID A0A1F3RHD0_9BACT Unreviewed; 224 AA.
AC A0A1F3RHD0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=tRNA (guanosine(18)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060};
DE EC=2.1.1.34 {ECO:0000256|HAMAP-Rule:MF_02060};
DE AltName: Full=tRNA [Gm18] methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060};
GN Name=trmH {ECO:0000256|HAMAP-Rule:MF_02060};
GN ORFNames=A3K10_05170 {ECO:0000313|EMBL:OFZ01604.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_31_6.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797363 {ECO:0000313|EMBL:OFZ01604.1, ECO:0000313|Proteomes:UP000176519};
RN [1] {ECO:0000313|EMBL:OFZ01604.1, ECO:0000313|Proteomes:UP000176519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in
CC tRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02060};
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000256|HAMAP-
CC Rule:MF_02060}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02060}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFZ01604.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MEPA01000025; OFZ01604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3RHD0; -.
DR Proteomes; UP000176519; Unassembled WGS sequence.
DR GO; GO:0141100; F:tRNA (guanine(18)-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; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR033671; TrmH.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR43453; RRNA METHYLASE-LIKE; 1.
DR PANTHER; PTHR43453:SF1; SPOU_METHYLASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060,
KW ECO:0000313|EMBL:OFZ01604.1};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_02060};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02060};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02060, ECO:0000313|EMBL:OFZ01604.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02060};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_02060}.
FT DOMAIN 34..177
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
SQ SEQUENCE 224 AA; 25538 MW; F547B99322503AD7 CRC64;
MKTDQEILDY LLSYATENKK KLFHQVIEKR TNHITVVLED IFQPHNASAV LRSCDVFGIQ
NVHIIENYNK YKINPKVVMG ASKWINMTKY NGAEDNTLRC INQLKADGYK IIATTPHHTD
CDITELPIED KTALLFGTEL QGLSKIALEN ADGFVKIPMY GFTESLNISV CAAISLYEIS
KRLKNSSINW QLTEEEKLQQ LLIWTKKIVK SSDLLINEFN ASVK
//
