RLMF_CITK8
ID RLMF_CITK8 Reviewed; 308 AA.
AC A8AIX5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=CKO_02316;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-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; CP000822; ABV13438.1; -; Genomic_DNA.
DR RefSeq; WP_012133165.1; NC_009792.1.
DR AlphaFoldDB; A8AIX5; -.
DR SMR; A8AIX5; -.
DR STRING; 290338.CKO_02316; -.
DR EnsemblBacteria; ABV13438; ABV13438; CKO_02316.
DR GeneID; 45136224; -.
DR KEGG; cko:CKO_02316; -.
DR HOGENOM; CLU_027534_3_0_6; -.
DR OMA; HQGRYDF; -.
DR OrthoDB; 1027015at2; -.
DR Proteomes; UP000008148; 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..308
FT /note="Ribosomal RNA large subunit methyltransferase F"
FT /id="PRO_0000349898"
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 34254 MW; E5886F591FAE0B47 CRC64;
MSAQKPGLHP RNRHHHRYDL ATLCQVTPEL AQFLTRTPAG EQSVDFANPL AVKALNKALL
AYFYQVANWD IPEGFLCPPV PGRADYIHHL ADLLGETTGA IPADASVLDV GTGANCIYPL
IGVHEYGWRF TGSEVHAQAL ASAQVIISGN PGLTRSIRLR RQKDPAAIFN GIIHKNEQYD
ATLCNPPFHD SAASARAGSE RKRRNLGQDK NDALNFGGQQ QELWCEGGEV AFIKTMIAES
QAFGRQVMWF TTLVSRGENL PPLYRALTDV GAVKVVKKEM AQGQKQSRFI AWTFMDDDQR
RRFMARKR
