RLMF_PECCP
ID RLMF_PECCP Reviewed; 311 AA.
AC C6D8Y7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=PC1_0640;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT11695.1; -; Genomic_DNA.
DR RefSeq; WP_012773342.1; NC_012917.1.
DR AlphaFoldDB; C6D8Y7; -.
DR SMR; C6D8Y7; -.
DR STRING; 561230.PC1_0640; -.
DR EnsemblBacteria; ACT11695; ACT11695; PC1_0640.
DR KEGG; pct:PC1_0640; -.
DR eggNOG; COG3129; Bacteria.
DR HOGENOM; CLU_027534_3_0_6; -.
DR OMA; HQGRYDF; -.
DR OrthoDB; 1027015at2; -.
DR Proteomes; UP000002736; 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..311
FT /note="Ribosomal RNA large subunit methyltransferase F"
FT /id="PRO_1000216112"
SQ SEQUENCE 311 AA; 35159 MW; 7AFA613D655A5F2C CRC64;
MTKPAVQKNG LHPRNRHRDR YDFPTLKHSY PALIPFVTVN AYGDESVDFA NPEAVKTLNQ
ALLQHFYQIE HWEIPDGFLC PPIPGRADYI HHLADLLAED NRAVVPREAS VLDIGCGANC
IYPLIGYREY GWRFTGSEIN PIAMKAANQT IEANPGLNRA IRLRRQKSST AILAGIIHKN
ETFDAVMCNP PFHASAEDAR QGSQRKLHNL GLDKRSPLNF GGQQDELWCE GGESAFIGQM
IKESAGFARQ CLWFTSLVSR KENLPEIYRA LEAVDAEKVR TIDMAQGQKQ SRFVAWSFLD
TAARTRWLQK R