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Database: UniProt
Entry: Q89YP0
LinkDB: Q89YP0
Original site: Q89YP0 
ID   RLMF_BACTN              Reviewed;         307 AA.
AC   Q89YP0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   13-FEB-2019, entry version 84.
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=BT_4691;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
OS   10582 / E50 / VPI-5482).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
CC   -!- FUNCTION: Specifically methylates the adenine in position 1618 of
CC       23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01848}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine =
CC         H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:16497, Rhea:RHEA-COMP:10229,
CC         Rhea:RHEA-COMP:10231, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC         EC=2.1.1.181; Evidence={ECO:0000255|HAMAP-Rule:MF_01848};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01848}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       METTL16/RlmF family. {ECO:0000255|HAMAP-Rule:MF_01848}.
DR   EMBL; AE015928; AAO79796.1; -; Genomic_DNA.
DR   RefSeq; NP_813602.1; NC_004663.1.
DR   RefSeq; WP_011109384.1; NC_004663.1.
DR   ProteinModelPortal; Q89YP0; -.
DR   SMR; Q89YP0; -.
DR   STRING; 226186.BT_4691; -.
DR   PaxDb; Q89YP0; -.
DR   PRIDE; Q89YP0; -.
DR   EnsemblBacteria; AAO79796; AAO79796; BT_4691.
DR   GeneID; 1071655; -.
DR   KEGG; bth:BT_4691; -.
DR   PATRIC; fig|226186.12.peg.4770; -.
DR   eggNOG; ENOG4105EBA; Bacteria.
DR   eggNOG; COG3129; LUCA.
DR   HOGENOM; HOG000218605; -.
DR   InParanoid; Q89YP0; -.
DR   KO; K06970; -.
DR   OMA; TEFHQGH; -.
DR   BioCyc; BTHE:G13PU-9676-MONOMER; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052907; F:23S rRNA (adenine(1618)-N(6))-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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;
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    307       Ribosomal RNA large subunit
FT                                methyltransferase F.
FT                                /FTId=PRO_0000349897.
SQ   SEQUENCE   307 AA;  35358 MW;  C7914E2A42C9C0B8 CRC64;
     MAERSELHTR NKHNGQYDFS LLTENYPPLR KFVLLNPLGI QTIDFFNPHA VKALNKALLI
     SYYGIRYWDI PRNYLCPPIP GRADYVHYIA DLIDPERVSN TANEENGDKP KRQCRCLDIG
     VGANCIYPII GHVEYGWMFV GSDIDPVSIE NARKIVTCNP VLAHKIDLRL QKDNRRIFDG
     IIAPDEYFDV TICNPPFHSS KKEAEEGTLR KLSSLKGEKV KKTKLNFGGN ANELWCEGGE
     LRFLLNMISE SRKYRKNCGW FTSLVSKEKN LDKLYAKLKA VHVSEYKIIR MCQGTKNSRI
     LAWRFLE
//
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