ID A0A0R1VSC7_9LACO Unreviewed; 222 AA.
AC A0A0R1VSC7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=FC15_GL000403 {ECO:0000313|EMBL:KRM08664.1};
OS Lapidilactobacillus concavus DSM 17758.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lapidilactobacillus.
OX NCBI_TaxID=1423735 {ECO:0000313|EMBL:KRM08664.1, ECO:0000313|Proteomes:UP000051315};
RN [1] {ECO:0000313|EMBL:KRM08664.1, ECO:0000313|Proteomes:UP000051315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17758 {ECO:0000313|EMBL:KRM08664.1,
RC ECO:0000313|Proteomes:UP000051315};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02217}.
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:KRM08664.1}.
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DR EMBL; AZFX01000080; KRM08664.1; -; Genomic_DNA.
DR RefSeq; WP_057825326.1; NZ_AZFX01000080.1.
DR AlphaFoldDB; A0A0R1VSC7; -.
DR STRING; 1423735.FC15_GL000403; -.
DR PATRIC; fig|1423735.3.peg.416; -.
DR OrthoDB; 9799672at2; -.
DR Proteomes; UP000051315; Unassembled WGS sequence.
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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02217}; Reference proteome {ECO:0000313|Proteomes:UP000051315};
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 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 121..122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
SQ SEQUENCE 222 AA; 25151 MW; BEA3425BF1857844 CRC64;
MRNEMMSRPV INSKVLHYLR QQPVPLSPKL KAIEAAAHQK RIPVIPHETV SYLYQLVDQL
HPRRVLEVGT AIGFSAALFV EASQMHAQVT TIDRYPEFYE QAKQNWQALG YQQSIQLMTG
DAADILPMLT GSYDLIFLDA AKAQYIHFLP EALRLLPPDG ILLIDDVLQA GTIFDPVETI
RHREKGIHRH LNQLLETVYD DPTLLVTLLP LGDGLLKITK RS
//
