TRML_LACGA
ID TRML_LACGA Reviewed; 185 AA.
AC Q042B4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Putative RNA (cytidine(34)-2'-O)-methyltransferase;
DE EC=2.1.1.207 {ECO:0000255|HAMAP-Rule:MF_01885};
DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885};
GN OrderedLocusNames=LGAS_1346;
OS Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS 102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=324831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC 3163 / NCIMB 11718 / NCTC 13722 / AM63;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- FUNCTION: Could methylate the ribose at the nucleotide 34 wobble
CC position in tRNA. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01885};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01885}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABJ60708.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000413; ABJ60708.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003646976.1; NZ_WBMG01000003.1.
DR AlphaFoldDB; Q042B4; -.
DR SMR; Q042B4; -.
DR GeneID; 66469420; -.
DR KEGG; lga:LGAS_1346; -.
DR HOGENOM; CLU_110125_0_0_9; -.
DR OrthoDB; 1578095at2; -.
DR BioCyc; LGAS324831:G1G6Y-1340-MON; -.
DR Proteomes; UP000000664; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008175; F:tRNA methyltransferase activity; 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; tRNA_cyt/urid_MeTfrase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42971; PTHR42971; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..185
FT /note="Putative RNA (cytidine(34)-2'-O)-methyltransferase"
FT /id="PRO_0000401946"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
SQ SEQUENCE 185 AA; 21690 MW; 8D358691A508C37F CRC64;
MTNHVVLYEP LMPANTGNIA RTCAGTNTIL DLIEPLGFQI DNKKMKRAGL DYWDKVDIRM
HDDLDAFLKT LGPNDEMYLI SKFSSKNYAQ VDYTDPNKDY YFVFGKETTG LPETFMREYY
DRNLRIPMSD NIRCYNLSNS VAMVLLEALR QQGFPNMETS HHYENDKLKD NYNRPERYER
NLGEN
