ID   RLMF_SHELP              Reviewed;         398 AA.
AC   A3QJF9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Shew_3741;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000606; ABO25607.1; -; Genomic_DNA.
DR   RefSeq; WP_011867535.1; NC_009092.1.
DR   AlphaFoldDB; A3QJF9; -.
DR   SMR; A3QJF9; -.
DR   STRING; 323850.Shew_3741; -.
DR   EnsemblBacteria; ABO25607; ABO25607; Shew_3741.
DR   KEGG; slo:Shew_3741; -.
DR   eggNOG; COG3129; Bacteria.
DR   HOGENOM; CLU_027534_3_0_6; -.
DR   OMA; HQGRYDF; -.
DR   OrthoDB; 1027015at2; -.
DR   Proteomes; UP000001558; 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; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..398
FT                   /note="Ribosomal RNA large subunit methyltransferase F"
FT                   /id="PRO_0000349957"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  43977 MW;  406EDFE8AA071260 CRC64;
     MTPSRKPARP GAKKVVSQEP SAKASRPKPS SQSKSKAQPK AKPESKPQAK SQAKPQAKSK
     PVEGKSQGAS KGLHPRNLHG QGYDFDALMD TTPELKPFVR PNPYGNLSID FADPRAVKLL
     NLALLRLHYG LSYWDIPEGF LCPPIPGRVD YLHYLADLLA ESTPASKGGK RKLPNVTRAP
     KGERVVALDI GTGANGIYPL LGHQVYGWRF VASDIDPVSL KNVERIIANN PQLAGKLSLR
     LQSDSKQIFT GIIRAEDRFD LTLCNPPFHA SLAEASRGSE RKLKNLAANK RAKGHEVAKS
     KEKLNFGGQK AELWCEGGEQ AFLGQMIRES QKFGSQCLWF TSLVSKKENL KPCYRLLEQV
     GAKRVETLEM AQGNKLTRVL AWTFLTPEQH SLWGLYRV