ID K1XE91_SPIPL Unreviewed; 274 AA. AC K1XE91; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 09-JAN-2013, entry version 2. DE SubName: Full=Dimethyladenosine transferase; GN ORFNames=SPLC1_S051420; OS Arthrospira platensis C1. OC Bacteria; Cyanobacteria; Oscillatoriales; Arthrospira. OX NCBI_TaxID=459495; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C1; RX PubMed=22675597; RA Cheevadhanarak S., Paithoonrangsarid K., Prommeenate P., Kaewngam W., RA Musigkain A., Tragoonrung S., Tabata S., Kaneko T., Chaijaruwanich J., RA Sangsrakru D., Tangphatsornruang S., Chanprasert J., Tongsima S., RA Kusonmano K., Jeamton W., Dulsawat S., Klanchui A., Vorapreeda T., RA Chumchua V., Khannapho C., Thammarongtham C., Plengvidhya V., RA Subudhi S., Hongsthong A., Ruengjitchatchawalya M., Meechai A., RA Senachak J., Tanticharoen M.; RT "Draft genome sequence of Arthrospira platensis C1 (PCC9438)."; RL Stand. Genomic Sci. 6:43-53(2012). CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 CC and A1519) in the loop of a conserved hairpin near the 3'-end of CC 16S rRNA in the 30S particle. May play a critical role in CC biogenesis of 30S subunits (By similarity). CC -!- CATALYTIC ACTIVITY: 4 S-adenosyl-L-methionine + CC adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L- CC homocysteine + N(6)-dimethyladenine(1518)/N(6)- CC dimethyladenine(1519) in 16S rRNA. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AFXD01000005; EKD10934.1; -; Genomic_DNA. DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro. DR GO; GO:0031167; P:rRNA methylation; IEA:GOC. DR Gene3D; 1.10.8.100; rRNA_Ade_diMease-like; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1; -. DR InterPro; IPR023165; rRNA_Ade_diMease-like. DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS. DR InterPro; IPR001737; rRNA_Ade_methylase_transferase. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR011530; rRNA_adenine_dimethylase. DR PANTHER; PTHR11727; PTHR11727; 1. DR Pfam; PF00398; RrnaAD; 1. DR SMART; SM00650; rADc; 1. DR TIGRFAMs; TIGR00755; ksgA; 1. DR PROSITE; PS01131; RRNA_A_DIMETH; 1. PE 3: Inferred from homology; KW Cytoplasm; Methyltransferase; RNA-binding; rRNA processing; KW S-adenosyl-L-methionine; Transferase. SQ SEQUENCE 274 AA; 30300 MW; 13B8E47D29FEF267 CRC64; MPSPQPRKRF AQHWLRSPAT LNHILEAADL SLGDRILEIG PGTGILTERL LPKVSSVVAV EIDRDLCVQL AKKFGKIDNF LLLQGDILNF DLNGYLSGFP KFQNPNKVVA NIPYNITGPI IEGLLGTIAK PAVKPFDAIV LLVQKEVGAR LCAKPSSKAF GALSVRVQYL AECDWICHVP ATAFYPPPKV DSAVVRLRPR PIASPAQNPQ LLETLVKLGF STRRKMLRNN LKSQVEPQTL NQLLETLDIN PQVRAEDLSL QQWVQLSNLL LAPQ //