ID A0A1E5SZB4_9BACT Unreviewed; 220 AA.
AC A0A1E5SZB4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BFP71_13390 {ECO:0000313|EMBL:OEK04462.1};
OS Roseivirga misakiensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1563681 {ECO:0000313|EMBL:OEK04462.1, ECO:0000313|Proteomes:UP000095552};
RN [1] {ECO:0000313|EMBL:OEK04462.1, ECO:0000313|Proteomes:UP000095552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-8 {ECO:0000313|EMBL:OEK04462.1,
RC ECO:0000313|Proteomes:UP000095552};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Fabibacter sp. strain SK-8.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:OEK04462.1}.
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DR EMBL; MDGQ01000005; OEK04462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5SZB4; -.
DR STRING; 1563681.BFP71_13390; -.
DR OrthoDB; 9794400at2; -.
DR Proteomes; UP000095552; 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 Reference proteome {ECO:0000313|Proteomes:UP000095552};
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};
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 25..167
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
SQ SEQUENCE 220 AA; 25562 MW; 207F2AF745C8B6F6 CRC64;
MLATYVTPNK LALIDKVLSE RTRHLTVVLE DIYHAQNASA VMRTCDCFGI QDLYITQRLH
DYEVNPNVVR GASKWITLHK YERESMSTEK CFKDLRKKNY RIVGTTPSSE VASIHELDLT
QKTAIVFGTE LGGLTKYARE QVDELVHVPM YGFTESFNIS VSAALILQEF VKRLKFSDIV
WQLTEKEQEE LKLEWFSRIV KRSDLHIKNY LKERSEKLEG
//
