ID K1XE91_ARTPT Unreviewed; 274 AA. AC K1XE91; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 19-JAN-2022, entry version 50. DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000256|HAMAP-Rule:MF_00607}; DE EC=2.1.1.182 {ECO:0000256|HAMAP-Rule:MF_00607}; 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 Microcoleaceae; Arthrospira. OX NCBI_TaxID=459495 {ECO:0000313|EMBL:EKD10934.1}; RN [1] {ECO:0000313|EMBL:EKD10934.1} 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., Subudhi S., RA Hongsthong A., Ruengjitchatchawalya M., Meechai A., Senachak J., RA 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 and CC A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA CC in the 30S particle. May play a critical role in biogenesis of 30S CC subunits. {ECO:0000256|HAMAP-Rule:MF_00607}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L- CC methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)- CC dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.182; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00607}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. rRNA adenine N(6)-methyltransferase family. RsmA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00607}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 RefSeq; WP_006621242.1; NZ_CM001632.1. DR STRING; 459495.SPLC1_S051420; -. DR EnsemblBacteria; EKD10934; EKD10934; SPLC1_S051420. DR PATRIC; fig|459495.6.peg.1030; -. DR eggNOG; COG0030; Bacteria. DR HOGENOM; CLU_041220_0_1_3; -. 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-UniRule. DR Gene3D; 1.10.8.100; -; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR023165; rRNA_Ade_diMease-like_C. 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_00607}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00607}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_00607}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_00607}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00607}. FT DOMAIN 20..201 FT /note="rADc" FT /evidence="ECO:0000259|SMART:SM00650" FT BINDING 13 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 15 FT /note="S-adenosyl-L-methionine; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 40 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 61 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 86 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" FT BINDING 111 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607, FT ECO:0000256|PROSITE-ProRule:PRU01026" 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 //