ID RLMF_COLP3 Reviewed; 301 AA. AC Q482M9; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 19. 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=CPS_2268; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic RT analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). 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; CP000083; AAZ28550.1; -; Genomic_DNA. DR RefSeq; YP_268988.1; -. DR GeneID; 3522810; -. DR GenomeReviews; CP000083_GR; CPS_2268. DR KEGG; cps:CPS_2268; -. DR NMPDR; fig|167879.3.peg.2205; -. DR TIGR; CPS_2268; -. DR HOGENOM; Q482M9; -. DR OMA; Q482M9; 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 1 301 Ribosomal RNA large subunit FT methyltransferase F. FT /FTId=PRO_0000349899. SQ SEQUENCE 301 AA; 34029 MW; A6A8292FC3745B7F CRC64; MHKKNRHNQG YNFTALVKAH PGLLQFIIKN QYNNQDTIDF ANPQAVKALN LSLLKSEYHV KFWDIPDGYL CPAIPGRVDY IHHLQDLLAA TPKTLLPNKT PINVLDIGTG ASCIYPILGQ REYDWHFVAS DVDPISIKVA KHIISSDKSL NRNINCRLQP NSNQIFNGII AEDEFYHLTI CNPPFHSSLA EASKGTARKI KNLNKGNHSS KNQDKTLNFG GQKAELWCPG GELAFIGKMI KESKAYQKQV LWFTCLVSKK DHLSKLKLSL KKSDAKQIKV IDMAQGQKIS RFIAWSFYDV N //