ID   RLMF_BACFR              Reviewed;         305 AA.
AC   Q64RQ5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=BF3081;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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}.
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DR   EMBL; AP006841; BAD49826.1; -; Genomic_DNA.
DR   RefSeq; WP_011203138.1; NC_006347.1.
DR   RefSeq; YP_100360.1; NC_006347.1.
DR   AlphaFoldDB; Q64RQ5; -.
DR   SMR; Q64RQ5; -.
DR   EnsemblBacteria; BAD49826; BAD49826; BF3081.
DR   KEGG; bfr:BF3081; -.
DR   PATRIC; fig|295405.11.peg.2947; -.
DR   HOGENOM; CLU_027534_3_0_10; -.
DR   OMA; HQGRYDF; -.
DR   Proteomes; UP000002197; 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..305
FT                   /note="Ribosomal RNA large subunit methyltransferase F"
FT                   /id="PRO_0000349895"
SQ   SEQUENCE   305 AA;  34823 MW;  187BA0521815A372 CRC64;
     MAERNELHKR NRHNGQYDFS RLTEEYPPLK KFIVLNAYGT TSIDFFNPRA VKALNKALLI
     SCYGIRYWDI PKNYLCPPIP GRADYIHYIA DLIQPDISDE STGLKTAIPN ARQYRCLDIG
     VGANCIYPII GQTEYGWTFV GSDIDPVSID NARKIVTCNP ALAHKIELRL QRDSRKIFEG
     IIAPNEYFDV TLCNPPFHSS KEEAEDGTLR KLSSLKGKKV TKARLNFGGN ANELWCEGGE
     LRFLLTMIEE SRNYRKNCGW FTSLVSKEKN LGKLTAKLKS TDIAEHRIIE MHQGTKTSRI
     LAWRF