RLMF_PSEAB
ID RLMF_PSEAB Reviewed; 336 AA.
AC Q02RZ9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=PA14_14340;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ13106.1; -; Genomic_DNA.
DR RefSeq; WP_003092887.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02RZ9; -.
DR SMR; Q02RZ9; -.
DR PRIDE; Q02RZ9; -.
DR EnsemblBacteria; ABJ13106; ABJ13106; PA14_14340.
DR KEGG; pau:PA14_14340; -.
DR HOGENOM; CLU_027534_3_0_6; -.
DR OMA; HQGRYDF; -.
DR BioCyc; PAER208963:G1G74-1178-MON; -.
DR Proteomes; UP000000653; 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..336
FT /note="Ribosomal RNA large subunit methyltransferase F"
FT /id="PRO_0000349927"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 37629 MW; 39176FDCAC7D679E CRC64;
MPRPTSPHPD AERKSASPLH PRNRHLGRYD FPRLIAGSPE LERFVILNPY GRQSIDFADP
AAVKAFNRAL LQQFYDVREW DIPDGYLCPP IPGRADYLHY LADLLGASHD GLIPRGPGLR
ALDVGTGANC IYPLLGHHEY GWRFVGADID PQSLASAAAI LAANPRFAAA IELRRQPDRR
QIFQGLIGVD ERFDMTLCNP PFHASLDEAT RGSRRKWKNL GKLDPTRTLP LLNFGGQGAE
LYCEGGEAAF LAGMAEESRA FATQVFWFTT LVSKASNLPN LQERLKTLGA SDIRVVDMAQ
GQKQSRFVAW TYLDKKQRRA WRKERWTAAL LEPLGE