ID A0A1T4JWG1_9FUSO Unreviewed; 210 AA.
AC A0A1T4JWG1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=tRNA 5-hydroxyuridine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02217};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_02217};
DE AltName: Full=ho5U methyltransferase {ECO:0000256|HAMAP-Rule:MF_02217};
GN Name=trmR {ECO:0000256|HAMAP-Rule:MF_02217};
GN ORFNames=SAMN02745174_00135 {ECO:0000313|EMBL:SJZ34488.1};
OS Cetobacterium ceti.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Cetobacterium.
OX NCBI_TaxID=180163 {ECO:0000313|EMBL:SJZ34488.1, ECO:0000313|Proteomes:UP000191153};
RN [1] {ECO:0000313|EMBL:SJZ34488.1, ECO:0000313|Proteomes:UP000191153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700028 {ECO:0000313|EMBL:SJZ34488.1,
RC ECO:0000313|Proteomes:UP000191153};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form
CC 5-methoxyuridine (mo5U) at position 34 in tRNAs. {ECO:0000256|HAMAP-
CC Rule:MF_02217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-
CC methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60524, Rhea:RHEA-COMP:13381, Rhea:RHEA-COMP:15591,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:136877, ChEBI:CHEBI:143860; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02217};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02217}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_02217}.
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DR EMBL; FUWX01000004; SJZ34488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4JWG1; -.
DR STRING; 180163.SAMN02745174_00135; -.
DR OrthoDB; 9799672at2; -.
DR Proteomes; UP000191153; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0016300; F:tRNA (uridine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_02217; TrmR_methyltr; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR InterPro; IPR043675; TrmR_methyltr.
DR PANTHER; PTHR10509:SF14; CATECHOL O-METHYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR10509; O-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02217};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02217};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02217}; Reference proteome {ECO:0000313|Proteomes:UP000191153};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02217};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02217}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_02217}.
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 114..115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
SQ SEQUENCE 210 AA; 24590 MW; 8A893D68BDC2CA67 CRC64;
MLEELKEANE YIIGKIKEED KLVLEMEEYA KEHNVPIVTK EVAEYLKFMI DINKSKNILE
VGTAIGYSGI LMGTVAKKYN GKLVTIEIDE ERYKLAQENF KKSGLDNITS ILGDATEEIK
KLDEEFDFVF IDASKGHYME FFNDSYKLLK KDGIIFIDNI MFRGYLYKEY PKRFKTIVRR
LDEFINYLYE NYNFTLVPFG DGIGLLKKED
//