ID D5C1D7_NITHN Unreviewed; 171 AA.
AC D5C1D7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=Nhal_3462 {ECO:0000313|EMBL:ADE16489.1};
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE16489.1, ECO:0000313|Proteomes:UP000001844};
RN [1] {ECO:0000313|Proteomes:UP000001844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01885}.
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DR EMBL; CP001798; ADE16489.1; -; Genomic_DNA.
DR RefSeq; WP_013034338.1; NC_013960.1.
DR AlphaFoldDB; D5C1D7; -.
DR STRING; 472759.Nhal_3462; -.
DR KEGG; nhl:Nhal_3462; -.
DR eggNOG; COG0219; Bacteria.
DR HOGENOM; CLU_110125_1_0_6; -.
DR OrthoDB; 9789043at2; -.
DR Proteomes; UP000001844; Chromosome.
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 NCBIfam; TIGR00185; tRNA_yibK_trmL; 1.
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:UP000001844};
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..142
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT REGION 152..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
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 122
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 130
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 171 AA; 19309 MW; D056B99F206B15E1 CRC64;
MFHIVLFEPE IPPNTGNIIR LCANTGAHLH LIQPLGFDLD DRRLRRAGLD YHEWARVKVH
PSLEHFSRRV QPRQVWACSS RGQQPYDKAH FHPGDALLFG PETRGLPRKL LNTLSPKQVL
RIPMLPASRS LNLSNAVAVV LYEAWRQHNF PGSRDAGEVA PEPHGDLISN G
//
