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Database: UniProt
Entry: A5F9W1_FLAJ1
LinkDB: A5F9W1_FLAJ1
Original site: A5F9W1_FLAJ1 
ID   A5F9W1_FLAJ1            Unreviewed;       220 AA.
AC   A5F9W1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   OrderedLocusNames=Fjoh_5009 {ECO:0000313|EMBL:ABQ08008.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ08008.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ08008.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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}.
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DR   EMBL; CP000685; ABQ08008.1; -; Genomic_DNA.
DR   RefSeq; WP_012026971.1; NZ_MUGZ01000004.1.
DR   AlphaFoldDB; A5F9W1; -.
DR   STRING; 376686.Fjoh_5009; -.
DR   KEGG; fjo:Fjoh_5009; -.
DR   eggNOG; COG0566; Bacteria.
DR   HOGENOM; CLU_021322_4_1_10; -.
DR   OrthoDB; 9785673at2; -.
DR   Proteomes; UP000006694; Chromosome.
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:ABQ08008.1};
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};
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          33..171
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
SQ   SEQUENCE   220 AA;  25492 MW;  1AB281E50792C6EE CRC64;
     MIDLDYLAFL EDILTDNRKE KFLKVLENRT KHFTIAVEDV YQMHNTSAVM RSCEVFGIQE
     LNIIEQRFGK RIDKEIALGA QKWVDINRFD TVDGCISSLR DKGYQIIATT PHENDCLIQD
     FDISKPSALF FGTEKDGLSP EILEKADGFL KIPMVGFTES LNISVSAAII IQNLTNRLRN
     SDIKWKLSDE EILQKRLDWA KNSIRDIKRI EARYYQDNPR
//
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