ID D2ZUY4_NEIMU Unreviewed; 134 AA.
AC D2ZUY4;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885};
DE EC=2.1.1.207 {ECO:0000256|HAMAP-Rule:MF_01885};
DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL {ECO:0000256|HAMAP-Rule:MF_01885};
GN Name=trmL {ECO:0000256|HAMAP-Rule:MF_01885};
GN ORFNames=NEIMUCOT_04425 {ECO:0000313|EMBL:EFC89140.1};
OS Neisseria mucosa ATCC 25996.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546266 {ECO:0000313|EMBL:EFC89140.1, ECO:0000313|Proteomes:UP000003344};
RN [1] {ECO:0000313|EMBL:EFC89140.1, ECO:0000313|Proteomes:UP000003344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25996 {ECO:0000313|EMBL:EFC89140.1,
RC ECO:0000313|Proteomes:UP000003344};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble position in
CC the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA).
CC Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH
CC of the wobble nucleotide. {ECO:0000256|HAMAP-Rule:MF_01885}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-
CC adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-
CC methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43088, Rhea:RHEA-COMP:10333, Rhea:RHEA-COMP:10334,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74508, ChEBI:CHEBI:74511; EC=2.1.1.207;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43084, Rhea:RHEA-COMP:10331, Rhea:RHEA-COMP:10332,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.207;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01885};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01885}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01885}.
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:EFC89140.1}.
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DR EMBL; ACDX02000004; EFC89140.1; -; Genomic_DNA.
DR AlphaFoldDB; D2ZUY4; -.
DR STRING; 546266.NEIMUCOT_04425; -.
DR eggNOG; COG0219; Bacteria.
DR Proteomes; UP000003344; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0141102; F:tRNA (5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0141098; F:tRNA (cytidine(34)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd18094; SpoU-like_TrmL; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_01885; tRNA_methyltr_TrmL; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR016914; TrmL.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42971; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR42971:SF1; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01885}; Reference proteome {ECO:0000313|Proteomes:UP000003344};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885,
KW ECO:0000256|PIRSR:PIRSR029256-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01885}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT DOMAIN 2..122
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885,
FT ECO:0000256|PIRSR:PIRSR029256-1"
SQ SEQUENCE 134 AA; 14793 MW; A7F960C30F9E17E6 CRC64;
MCANTGADLH LVKPLGFPLD SAKMKRAGLD YHEFAKLTVH ENFEDCLKAL EGRRIFALTT
KGKTRPDKVS FVEGDVFLFG PETRGLPAEI LDTLPEGQKL RLPMKLGSRS MNLSNTVAVI
LFEAWRQNGY AGGV
//
