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RLMF_SHEPC
ID   RLMF_SHEPC              Reviewed;         357 AA.
AC   A4Y1N1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, 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};
GN   OrderedLocusNames=Sputcn32_0128;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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; CP000681; ABP73864.1; -; Genomic_DNA.
DR   RefSeq; WP_011791170.1; NC_009438.1.
DR   AlphaFoldDB; A4Y1N1; -.
DR   SMR; A4Y1N1; -.
DR   STRING; 319224.Sputcn32_0128; -.
DR   GeneID; 45040568; -.
DR   KEGG; spc:Sputcn32_0128; -.
DR   eggNOG; COG3129; Bacteria.
DR   HOGENOM; CLU_027534_3_0_6; -.
DR   OMA; HQGRYDF; -.
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..357
FT                   /note="Ribosomal RNA large subunit methyltransferase F"
FT                   /id="PRO_0000349960"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  39438 MW;  BFD1A92ED24C8ED4 CRC64;
     MPKPPRSTQI LSCNAPNGKP KTQHPSARAK VKRTPVNTRS IAEIKKALHP RNVHINGYDF
     NALIKAFPRL NAFVRPTSFG GLSIDFADPE AVKTLNTALL KHHYGIDFWD IPKGALCPPI
     PGRVDYLHYL ADLLAEGDHH LVMDRVSVLD IGTGANGIYP ILGCQVFGWH FVASDINSIS
     LANVQGIIAQ NPALHGRLNL RLQGDESAIF KGVIQPQERF ELTLCNPPFH ASLAEAAEGS
     LRKVRNLQLN RGRTAKPVAK LNFGGQGAEL WCQGGEPQFL ATMIDESQAF ADQCLWFTSL
     VSKKENLKPC YQALAKLAVD TVKTIEMQQG NKMTRILAWS FQSAAKRKIW RNAHLSD
 
 
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