ID   RLMF_ALIF1              Reviewed;         319 AA.
AC   Q5DYC3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=VF_A1153;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000021; AAW88223.1; -; Genomic_DNA.
DR   RefSeq; WP_011263945.1; NC_006841.2.
DR   RefSeq; YP_207111.1; NC_006841.2.
DR   AlphaFoldDB; Q5DYC3; -.
DR   SMR; Q5DYC3; -.
DR   STRING; 312309.VF_A1153; -.
DR   EnsemblBacteria; AAW88223; AAW88223; VF_A1153.
DR   KEGG; vfi:VF_A1153; -.
DR   PATRIC; fig|312309.11.peg.3753; -.
DR   eggNOG; COG3129; Bacteria.
DR   HOGENOM; CLU_027534_3_0_6; -.
DR   OMA; HQGRYDF; -.
DR   OrthoDB; 1027015at2; -.
DR   Proteomes; UP000000537; Chromosome II.
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; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..319
FT                   /note="Ribosomal RNA large subunit methyltransferase F"
FT                   /id="PRO_0000349975"
SQ   SEQUENCE   319 AA;  35702 MW;  E3DEFF083C95571E CRC64;
     MTNTKSNVTK KSLHPRNKHT GNYDFPALIK ACAELKPFVE TNQYGNESIN FSDPQAVKAL
     NKALLAHFYN VPFWDIPQGY LCPPIPGRAD YIHNIADLLA ITNEGTIPTG KKVKGLDVGV
     GANCVYLIIG NREYQWSFVG SDIDPQSIKM ASFIANNNPS LKGIECRLQK NEENIFKGII
     KPTEFFDFTM CNPPFHASEA EATAGTERKQ KNLAANKAKK GHAFQEMQNA KALNFGGQKA
     ELWCEGGELA FILKMAQQSR EFSLQVQWFT TLISKKENVA ELYKELEKIG VKTIKTIEMA
     QGQKISRFVA WTYQANVNL