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RLMF_SHIB3
ID   RLMF_SHIB3              Reviewed;         308 AA.
AC   B2TVC2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
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};
GN   OrderedLocusNames=SbBS512_E2543;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACD08252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001063; ACD08252.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001275941.1; NC_010658.1.
DR   AlphaFoldDB; B2TVC2; -.
DR   SMR; B2TVC2; -.
DR   STRING; 344609.SbBS512_E2543; -.
DR   EnsemblBacteria; ACD08252; ACD08252; SbBS512_E2543.
DR   GeneID; 66670921; -.
DR   KEGG; sbc:SbBS512_E2543; -.
DR   HOGENOM; CLU_027534_3_0_6; -.
DR   OMA; HQGRYDF; -.
DR   Proteomes; UP000001030; 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_0000349967"
SQ   SEQUENCE   308 AA;  34180 MW;  10D0EA4C2F3E23D3 CRC64;
     MSAQKPGLHP RNRHHSRYDL ATLCQVNPEL RQFLTLTPAG EQSVDFANPL AVKALNKALL
     AHFYAVANWD IPDGFLCPPV PGRADYIHHL ADLLAEASGT IPANASILDI GVGANCIYPL
     IGVHEYGWRF TGSETSSQAL SSAQAIISAN PGLNRAIRLR RQKESGAIFN GIIHKNEQYD
     ATLCNPPFHD SAAAARAGSE RKRRNLGLNK DDALNFGGQQ QELWCEGGEV AFIKKMIEES
     KGFAKQVMWF TSLVSRGENL PPLYRALTDV GAVKVVKKEM AQGQKQSRFI AWTFMNDEQR
     RRFVNRQR
 
 
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