RLMF_DESPS
ID RLMF_DESPS Reviewed; 309 AA.
AC Q6ANQ6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=DP1289;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR522870; CAG36018.1; -; Genomic_DNA.
DR RefSeq; WP_011188530.1; NC_006138.1.
DR AlphaFoldDB; Q6ANQ6; -.
DR SMR; Q6ANQ6; -.
DR STRING; 177439.DP1289; -.
DR EnsemblBacteria; CAG36018; CAG36018; DP1289.
DR KEGG; dps:DP1289; -.
DR eggNOG; COG3129; Bacteria.
DR HOGENOM; CLU_027534_3_0_7; -.
DR OMA; HQGRYDF; -.
DR OrthoDB; 1027015at2; -.
DR Proteomes; UP000000602; 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..309
FT /note="Ribosomal RNA large subunit methyltransferase F"
FT /id="PRO_0000349902"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 34541 MW; E44C3EBD267BC0AE CRC64;
MASQHDKKSV QSGLLHPRNP HRGRYDLDAL CRTCPELKMH IQIKPTGDKT IDFSDAKAVL
CLNRALLAHY YQVSNWQIPE GYLCPPIPGR ADYIHYLADL LAEDLPTSAK GKKIRVLDIG
TGANCIYPII GSQSYGWHFV GTDIDPLAIK IAGMIVQANS CLNGKITLKQ QLDKKLIFKG
IINEDKFDLT MCNPPFHASL AEAEAGNQRK RKNLGHGKEN RAQEKLNFGG QNAELWCPGG
EIVFLRQMAE ESVAFAKQVR WFSSLLSKGK NVAPLKKLLK QLGCKRIKVV EMAQGQKISR
FIAWSFSQE
