ID RLMF_SHEFN Reviewed; 360 AA. AC Q08A02; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Ribosomal RNA large subunit methyltransferase F; DE EC=2.1.1.48; DE AltName: Full=23S rRNA mA1618 methyltransferase; DE AltName: Full=rRNA adenine N-6-methyltransferase; GN Name=rlmF; OrderedLocusNames=Sfri_0050; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., RA Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F., RA Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Shewanella frigidimarina NCIMB 400."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates the adenine in position 1618 of CC 23S rRNA (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + rRNA = S-adenosyl-L- CC homocysteine + rRNA containing N(6)-methyladenine. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC METT10D/rlmF family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000447; ABI69913.1; -; Genomic_DNA. DR RefSeq; YP_748751.1; -. DR GeneID; 4278257; -. DR GenomeReviews; CP000447_GR; Sfri_0050. DR KEGG; sfr:Sfri_0050; -. DR NMPDR; fig|318167.10.peg.51; -. DR HOGENOM; Q08A02; -. DR OMA; Q08A02; LNFGGQN. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008988; F:rRNA (adenine-N6-)-methyltransferase activity; IEA:HAMAP. DR GO; GO:0000154; P:rRNA modification; IEA:InterPro. DR HAMAP; MF_01848; -; 1. DR InterPro; IPR016909; S-AdoMet-dep_MeTrfase_YbiN_prd. DR InterPro; IPR010286; SAM-Mtase_prd. DR PANTHER; PTHR13393; DUF890; 1. DR Pfam; PF05971; Methyltransf_10; 1. DR PIRSF; PIRSF029038; Mtase_YbiN_prd; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; rRNA processing; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 360 Ribosomal RNA large subunit FT methyltransferase F. FT /FTId=PRO_0000349955. SQ SEQUENCE 360 AA; 39753 MW; AE375BD772BD1BDA CRC64; MTRSTTPPMR AKHSSAKRSP SRSAAKVNPV SVKPNKPLLS KALHPRNAHL QGYDFATLII AMPALAAFVR PNPYGNPSID FADPKAVKSL NAALLLSEYH INGWDIPEGY LCPPVPGRVD YLHYIADLLA VKGKVVKGAS IRGLDIGTGA NGIYPLLGIQ TYGWQFVASD IDPVSIDNVA KIAQQNEKIT AHLQLRLQPQ PEHIFKNIIA ADERFDVTLC NPPFHSSLAE ASEGSLRKVK NLAKNQQQKH GQQSRKLAVS QAKPTLNFGG QKAELWCQGG EQQFLANMIK QSRDYANQVL WFTSLVSKSD NLKPCYQLLK QLNAVEVKTI EMTQGNKATR ILAWSFLTPA IHQQWATLRP //