ID W6S4Q7_9CYAN Unreviewed; 274 AA. AC W6S4Q7; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JAN-2015, entry version 8. 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=ksgA {ECO:0000256|HAMAP-Rule:MF_00607}; GN Synonyms=rsmA {ECO:0000256|HAMAP-Rule:MF_00607}; GN ORFNames=ARTHRO_11116 {ECO:0000313|EMBL:CDM93443.1}; OS Arthrospira sp. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Arthrospira. OX NCBI_TaxID=35824 {ECO:0000313|EMBL:CDM93443.1}; RN [1] {ECO:0000313|EMBL:CDM93443.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PCC 8005 {ECO:0000313|EMBL:CDM93443.1}; RA Genoscope - CEA; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; FO818640; CDM93443.1; -; Genomic_DNA. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00015091}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00058353}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00058343}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00058329}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00058334}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00607, KW ECO:0000256|SAAS:SAAS00058351}. 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 //