ID C8NJ01_9LACT Unreviewed; 169 AA.
AC C8NJ01;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Putative 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 {ECO:0000256|HAMAP-Rule:MF_01885};
GN ORFNames=HMPREF0444_1896 {ECO:0000313|EMBL:EEW36548.1};
OS Granulicatella adiacens ATCC 49175.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Granulicatella.
OX NCBI_TaxID=638301 {ECO:0000313|EMBL:EEW36548.1, ECO:0000313|Proteomes:UP000005926};
RN [1] {ECO:0000313|EMBL:EEW36548.1, ECO:0000313|Proteomes:UP000005926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49175 {ECO:0000313|EMBL:EEW36548.1,
RC ECO:0000313|Proteomes:UP000005926};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Could methylate the ribose at the nucleotide 34 wobble
CC position in tRNA. {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 -!- 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:EEW36548.1}.
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DR EMBL; ACKZ01000029; EEW36548.1; -; Genomic_DNA.
DR RefSeq; WP_005606569.1; NZ_GG694016.1.
DR AlphaFoldDB; C8NJ01; -.
DR STRING; 638301.HMPREF0444_1896; -.
DR eggNOG; COG0219; Bacteria.
DR HOGENOM; CLU_110125_0_0_9; -.
DR Proteomes; UP000005926; 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 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|HAMAP-Rule:MF_01885,
KW ECO:0000313|EMBL:EEW36548.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005926};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885,
KW ECO:0000256|PIRSR:PIRSR029256-1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01885, ECO:0000313|EMBL:EEW36548.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT DOMAIN 5..146
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
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 104
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 125
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 134
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 169 AA; 19586 MW; 7582413C3D1E563D CRC64;
MTVNHIVLFE PQIPANTGNI ARTCAATNSP LHLIEPLGFS TDDKHLKRAG LDYWHDVDIT
YHKSMEAFLD YLGERPLYLI TKFANHTYDE VDLARDEEQF FMFGKETTGL PEEFMRENEE
KCLRLPMNDT HVRSLNLSNT AAIVVYEALR QQRFAGLELV HTYDHDKLK
//
