(data stored in SCRATCH3701 zone)

SWISSPROT: RLMF_ECOBW

ID   RLMF_ECOBW              Reviewed;         308 AA.
AC   C4ZXX9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 56.
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=BWG_0660;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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}.
DR   EMBL; CP001396; ACR65092.1; -; Genomic_DNA.
DR   SMR; C4ZXX9; -.
DR   EnsemblBacteria; ACR65092; ACR65092; BWG_0660.
DR   KEGG; ebw:BWG_0660; -.
DR   HOGENOM; HOG000218605; -.
DR   KO; K06970; -.
DR   OMA; TEFHQGH; -.
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   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.
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;
DR   PRODOM; C4ZXX9.
DR   SWISS-2DPAGE; C4ZXX9.
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_1000216111"
SQ   SEQUENCE   308 AA;  34226 MW;  E096A6624F37D546 CRC64;
     MSAQKPGLHP RNRHHSRYDL ATLCQVNPEL RQFLTLTPAG EQSVDFANPL AVKALNKALL
     AHFYAVANWD IPDGFLCPPV PGRADYIHHL ADLLAEASGT IPANASILDI GVGANCIYPL
     IGVHEYGWRF TGSETSSQAL SSAQAIISSN PGLNRAIRLR RQKESGAIFN GIIHKNEQYD
     ATLCNPPFHD SAAAARAGSE RKRRNLGLNK DDALNFGGQQ QELWCEGGEV TFIKKMIEES
     KGFAKQVMWF TSLVSRGENL PPLYRALTDV GAVKVVKKEM AQGQKQSRFI AWTFMNDEQR
     RRFVNRQR
//

If you have problems or comments...

PBIL Back to PBIL home page