RLMF_BACTN
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 03-AUG-2022, entry version 96.
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=BT_4691;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
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 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA 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 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; AE015928; AAO79796.1; -; Genomic_DNA.
DR RefSeq; NP_813602.1; NC_004663.1.
DR RefSeq; WP_011109384.1; NC_004663.1.
DR AlphaFoldDB; Q89YP0; -.
DR SMR; Q89YP0; -.
DR STRING; 226186.BT_4691; -.
DR PaxDb; Q89YP0; -.
DR PRIDE; Q89YP0; -.
DR EnsemblBacteria; AAO79796; AAO79796; BT_4691.
DR GeneID; 60925863; -.
DR KEGG; bth:BT_4691; -.
DR PATRIC; fig|226186.12.peg.4770; -.
DR eggNOG; COG3129; Bacteria.
DR HOGENOM; CLU_027534_3_0_10; -.
DR InParanoid; Q89YP0; -.
DR OMA; HQGRYDF; -.
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 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..307
FT /note="Ribosomal RNA large subunit methyltransferase F"
FT /id="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
