RLMF_PECAS
ID RLMF_PECAS Reviewed; 311 AA.
AC Q6D958;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=ECA0761;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(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}.
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DR EMBL; BX950851; CAG73675.1; -; Genomic_DNA.
DR RefSeq; WP_011092368.1; NC_004547.2.
DR AlphaFoldDB; Q6D958; -.
DR SMR; Q6D958; -.
DR STRING; 218491.ECA0761; -.
DR EnsemblBacteria; CAG73675; CAG73675; ECA0761.
DR GeneID; 57207491; -.
DR KEGG; eca:ECA0761; -.
DR PATRIC; fig|218491.5.peg.759; -.
DR eggNOG; COG3129; Bacteria.
DR HOGENOM; CLU_027534_3_0_6; -.
DR OMA; HQGRYDF; -.
DR OrthoDB; 1027015at2; -.
DR Proteomes; UP000007966; 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..311
FT /note="Ribosomal RNA large subunit methyltransferase F"
FT /id="PRO_0000349905"
SQ SEQUENCE 311 AA; 35095 MW; 079B2D94152D50A2 CRC64;
MTKPAVQKSG LHPRNRHRDR YDFPALKQSY PALIPFVKVN AYGDESVDFA NPEAVKTLNQ
ALLQHFYQIE HWTIPDGFLC PPIPGRADYV HHLADLLAED NRSVVPRDAS VLDVGCGANC
VYPLIGHREY GWRFTGSEVN PLAMKAANET IEANSGLNRS IRLRRQKNSK AILAGIIHKN
DSFDAVMCNP PFHASAEDAR EGSQRKLHNL GLDKRSPLNF GGQQDELWCE GGELAFIGQM
IKDSVSFGRQ CLWFTSLVSR KEHLPEIYRA LEAVDAEKVR TIDMAQGQKQ SRFVAWSFLD
TAARARWLQK R