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Database: UniProt
Entry: F9RCS6_VIBSN
LinkDB: F9RCS6_VIBSN
Original site: F9RCS6_VIBSN 
ID   F9RCS6_VIBSN            Unreviewed;       227 AA.
AC   F9RCS6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=VIBRN418_01081 {ECO:0000313|EMBL:EGU33678.1};
OS   Vibrio sp. (strain N418).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU33678.1, ECO:0000313|Proteomes:UP000003627};
RN   [1] {ECO:0000313|EMBL:EGU33678.1, ECO:0000313|Proteomes:UP000003627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N418 {ECO:0000313|EMBL:EGU33678.1,
RC   ECO:0000313|Proteomes:UP000003627};
RA   Strain E.A., Brown E., Allard M.W.;
RL   Submitted (AUG-2011) 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:EGU33678.1}.
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DR   EMBL; AFWD01000052; EGU33678.1; -; Genomic_DNA.
DR   RefSeq; WP_009386221.1; NZ_AFWD01000052.1.
DR   AlphaFoldDB; F9RCS6; -.
DR   eggNOG; COG0566; Bacteria.
DR   OMA; YQHVRHH; -.
DR   Proteomes; UP000003627; Unassembled WGS sequence.
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; 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; IPR022724; rRNA_MeTrfase_SpoU_C.
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; PF12105; SpoU_methylas_C; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_02060};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_02060};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_02060};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02060};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_02060};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_02060}.
FT   DOMAIN          20..158
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
FT   DOMAIN          162..217
FT                   /note="RNA methyltransferase SpoU/TrmH type C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12105"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT   BINDING         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
SQ   SEQUENCE   227 AA;  25454 MW;  3FEBAB461078E495 CRC64;
     MNLERYNRIQ QVLKARQTDL TFCLEEVHKP NNVSAVIRTA DATGIHKIHA VWPAKMRTLT
     HTSAGARNWV EVDTHSSIDD AIGELKAQGM QILVTNLSDT AVDFRQIDYT KPTAIILGSE
     KVGASARAKE LADQDIIIPM MGMVQSLNVS VASAVIMYEA QRQREAAGMY DRETSPLSEE
     VINRILFERG HPVLAKVAKR KKMPYPPLDD EGQIVADDDW WAEMQKK
//
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