ID   RLMF_SHIF8              Reviewed;         308 AA.
AC   Q0T6F4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase F {ECO:0000255|HAMAP-Rule:MF_01848};
DE            EC=2.1.1.181 {ECO:0000255|HAMAP-Rule:MF_01848};
DE   AltName: Full=23S rRNA mA1618 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01848};
DE   AltName: Full=rRNA adenine N-6-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01848};
GN   Name=rlmF {ECO:0000255|HAMAP-Rule:MF_01848}; OrderedLocusNames=SFV_0791;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: Specifically methylates the adenine in position 1618 of 23S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01848}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16497, Rhea:RHEA-COMP:10229, Rhea:RHEA-COMP:10231,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.181;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01848};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01848}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL16/RlmF
CC       family. {ECO:0000255|HAMAP-Rule:MF_01848}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF03022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000266; ABF03022.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001343936.1; NC_008258.1.
DR   AlphaFoldDB; Q0T6F4; -.
DR   SMR; Q0T6F4; -.
DR   EnsemblBacteria; ABF03022; ABF03022; SFV_0791.
DR   KEGG; sfv:SFV_0791; -.
DR   HOGENOM; CLU_027534_3_0_6; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052907; F:23S rRNA (adenine(1618)-N(6))-methyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01848; 23SrRNA_methyltr_F; 1.
DR   InterPro; IPR010286; METTL16/RlmF.
DR   InterPro; IPR016909; rRNA_lsu_MeTfrase_F.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13393; PTHR13393; 1.
DR   Pfam; PF05971; Methyltransf_10; 1.
DR   PIRSF; PIRSF029038; Mtase_YbiN_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..308
FT                   /note="Ribosomal RNA large subunit methyltransferase F"
FT                   /id="PRO_0000349971"
SQ   SEQUENCE   308 AA;  34223 MW;  1B00E19C2F32DC20 CRC64;
     MSAQKPGLHP RNRHHSRYDL ATLCQVNPEL RQFLTLTPAG EQSVDFANPL AVKALNKALL
     AHFYAVANWD IPDGFLCPPV PGRADYIHHL ADLLAEASGT IPANASILDI GVGANCIYPL
     IGVHEYGWRF TGSETSSQAL SSAQAIISAN PGLNRAIRLR RQKESGAIFN GIIHKNEQYD
     ATLCNPPFHD SAAAARAGSE RKRRNLGLNK DDALNFGGQQ QELWCEGGEV NFIKKMIEES
     KGFAKQVMWF TSLVSRGENL PPLYRALTDV GAVKVVKKEM AQGQKQSRFI AWTFMNDEQR
     RRFVNRQR