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Database: UniProt
Entry: E1WXK8_HALMS
LinkDB: E1WXK8_HALMS
Original site: E1WXK8_HALMS 
ID   E1WXK8_HALMS            Unreviewed;       249 AA.
AC   E1WXK8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   ECO:0000313|EMBL:CBW27526.1};
GN   OrderedLocusNames=BMS_2750 {ECO:0000313|EMBL:CBW27526.1};
OS   Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS   (Bacteriovorax marinus).
OC   Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC   Halobacteriovoraceae; Halobacteriovorax.
OX   NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW27526.1, ECO:0000313|Proteomes:UP000008963};
RN   [1] {ECO:0000313|Proteomes:UP000008963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC   {ECO:0000313|Proteomes:UP000008963};
RX   PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA   Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA   Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA   Williams H.N., Stine O.C.;
RT   "A small predatory core genome in the divergent marine Bacteriovorax
RT   marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL   ISME J. 7:148-160(2013).
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; FQ312005; CBW27526.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1WXK8; -.
DR   STRING; 862908.BMS_2750; -.
DR   KEGG; bmx:BMS_2750; -.
DR   PATRIC; fig|862908.3.peg.2626; -.
DR   eggNOG; COG0566; Bacteria.
DR   HOGENOM; CLU_021322_4_1_7; -.
DR   Proteomes; UP000008963; 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   Reference proteome {ECO:0000313|Proteomes:UP000008963};
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          61..199
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT   BINDING         180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT   BINDING         189
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
SQ   SEQUENCE   249 AA;  28628 MW;  2CA7CD5C76CA7C68 CRC64;
     MRTAVYSTKI MKVVFKAHEE KLEINDKNFD HHTMRSIVED SLNDQRKELI ERILDQRISG
     LSVILESLGD LGNLQAISRT CDNFGVQKLE IIETKGPMKW TNRTSQGAHK WVTMQKWYET
     KDCLQYFKDR GVQIVSTAFS DKAIPYTEVD FTKPTALLMG NESFGISEVA REMSDVECII
     PSYGYSQSLN VSVAAAIVIE HATSQIRKAH QGGGDFNEEQ REFFKSFFYF QANQYSRALM
     REHFKKKAL
//
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