ID K1XE91_ARTPT Unreviewed; 274 AA. AC K1XE91; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 04-FEB-2015, entry version 20. DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|SAAS:SAAS00015019}; DE EC=2.1.1.182 {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|SAAS:SAAS00015085}; DE AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000256|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethylase {ECO:0000256|HAMAP-Rule:MF_00607}; DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607}; GN Name=rsmA {ECO:0000256|HAMAP-Rule:MF_00607}; GN Synonyms=ksgA {ECO:0000256|HAMAP-Rule:MF_00607}; GN ORFNames=SPLC1_S051420 {ECO:0000313|EMBL:EKD10934.1}; OS Arthrospira platensis C1. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=459495 {ECO:0000313|EMBL:EKD10934.1, ECO:0000313|Proteomes:UP000006749}; RN [1] {ECO:0000313|EMBL:EKD10934.1, ECO:0000313|Proteomes:UP000006749} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C1 {ECO:0000313|EMBL:EKD10934.1}; 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. {ECO:0000256|HAMAP-Rule:MF_00607, CC ECO:0000256|SAAS:SAAS00015064}. 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. {ECO:0000256|HAMAP- CC Rule:MF_00607, ECO:0000256|SAAS:SAAS00015030}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607, CC ECO:0000256|SAAS:SAAS00015039}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. rRNA adenine N(6)-methyltransferase CC family. RsmA subfamily. {ECO:0000256|HAMAP-Rule:MF_00607}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKD10934.1}. 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 EnsemblBacteria; EKD10934; EKD10934; SPLC1_S051420. DR Proteomes; UP000006749; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro. DR Gene3D; 1.10.8.100; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR023165; rRNA_Ade_diMease-like. DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR011530; rRNA_adenine_dimethylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11727; PTHR11727; 1. DR Pfam; PF00398; RrnaAD; 1. DR SMART; SM00650; rADc; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00755; ksgA; 1. DR PROSITE; PS01131; RRNA_A_DIMETH; 1. DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006749}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00015091}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00021807}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00021841}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00021802}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00021823}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00021805}. FT BINDING 13 13 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00607}. FT BINDING 15 15 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_00607}. FT BINDING 40 40 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00607}. FT BINDING 61 61 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00607}. FT BINDING 86 86 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00607}. FT BINDING 111 111 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00607}. 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 //