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RLMF_SALG2
ID   RLMF_SALG2              Reviewed;         308 AA.
AC   B5R792;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=SG0804;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR36699.1; -; Genomic_DNA.
DR   RefSeq; WP_001275962.1; NC_011274.1.
DR   AlphaFoldDB; B5R792; -.
DR   SMR; B5R792; -.
DR   EnsemblBacteria; CAR36699; CAR36699; SG0804.
DR   KEGG; seg:SG0804; -.
DR   HOGENOM; CLU_027534_3_0_6; -.
DR   OMA; HQGRYDF; -.
DR   Proteomes; UP000008321; 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_1000188531"
SQ   SEQUENCE   308 AA;  34310 MW;  F854E876812802B9 CRC64;
     MSAQKPGLHP RNRHQHRYDL AALCQTTPEL TSFLIRTPAG EQSVDFANPQ AVKALNKALL
     AHFYAVTHWD IPPGFLCPPV PGRADYIHHL ADLLGETTGS IPAQATILDV GVGANCIYPL
     IGVHEYGWRF TGSEVSDAAM SSAQAIIQAN TGLSRAIRLR RQKDPAAIFT GIIHKNEFYD
     ATLCNPPFHD SAAAARAGSE RKRRNLGQNK DDALNFGGQQ QELWCEGGEV AFIKKMIAES
     QSFRRQVLWF TTLVSRGENL PPLYRALTEA GAVKVVKKEM AQGQKQSRFI AWTFMDDDQR
     RRFITRKR
 
 
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