ID Q8DQY3_STRR6 Unreviewed; 180 AA.
AC Q8DQY3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 106.
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 Name=cspR {ECO:0000313|EMBL:AAK99236.1};
GN OrderedLocusNames=spr0432 {ECO:0000313|EMBL:AAK99236.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99236.1, ECO:0000313|Proteomes:UP000000586};
RN [1] {ECO:0000313|EMBL:AAK99236.1, ECO:0000313|Proteomes:UP000000586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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}.
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DR EMBL; AE007317; AAK99236.1; -; Genomic_DNA.
DR PIR; H97925; H97925.
DR RefSeq; NP_358026.1; NC_003098.1.
DR AlphaFoldDB; Q8DQY3; -.
DR STRING; 171101.spr0432; -.
DR KEGG; spr:spr0432; -.
DR PATRIC; fig|171101.6.peg.475; -.
DR eggNOG; COG0219; Bacteria.
DR HOGENOM; CLU_110125_0_0_9; -.
DR Proteomes; UP000000586; 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:0002131; P:wobble position cytosine ribose methylation; IBA:GO_Central.
DR GO; GO:0002132; P:wobble position uridine ribose methylation; IBA:GO_Central.
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|HAMAP-Rule:MF_01885,
KW ECO:0000313|EMBL:AAK99236.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000586};
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:AAK99236.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT DOMAIN 17..157
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT BINDING 91
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 115
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 136
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 145
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 180 AA; 21179 MW; 2FAC04038B271EA5 CRC64;
MWLFFCNGKR KQVMTNHIVL FEPQIPQNTG NIARTCAATN SPLHIIKPMG FPIDDRKMKR
AGLDYWDKLE IYFYESLEDF MSQMKGKLYL ISKFAEKVYS DVDLSTNEDH YFLFGREDKG
LPEDFMREHP EKALRIPMND EHVRSLNVSN TVCMIVYEAL RQQNFAGLEL VHTYEVDKLK
//
