ID   RSMA_METHJ              Reviewed;         256 AA.
AC   Q2FSA9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000255|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethylase {ECO:0000255|HAMAP-Rule:MF_00607};
DE   AltName: Full=S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607};
GN   Name=rsmA {ECO:0000255|HAMAP-Rule:MF_00607};
GN   Synonyms=ksgA {ECO:0000255|HAMAP-Rule:MF_00607};
GN   OrderedLocusNames=Mhun_3029;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
CC   -!- FUNCTION: Specifically dimethylates two adjacent adenosines in the loop
CC       of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle.
CC       May play a critical role in biogenesis of 30S subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00607}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00607}.
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DR   EMBL; CP000254; ABD42716.1; -; Genomic_DNA.
DR   RefSeq; WP_011449967.1; NC_007796.1.
DR   AlphaFoldDB; Q2FSA9; -.
DR   SMR; Q2FSA9; -.
DR   STRING; 323259.Mhun_3029; -.
DR   EnsemblBacteria; ABD42716; ABD42716; Mhun_3029.
DR   GeneID; 3922930; -.
DR   KEGG; mhu:Mhun_3029; -.
DR   eggNOG; arCOG04131; Archaea.
DR   HOGENOM; CLU_041220_0_2_2; -.
DR   OMA; KEEEPYF; -.
DR   OrthoDB; 99734at2157; -.
DR   Proteomes; UP000001941; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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_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_sf.
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; Methyltransferase; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..256
FT                   /note="Probable ribosomal RNA small subunit
FT                   methyltransferase A"
FT                   /id="PRO_0000257382"
FT   BINDING         8
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         10
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
SQ   SEQUENCE   256 AA;  28902 MW;  3E6EE2964A7CE277 CRC64;
     MRAYRDQHFL TDPRIVARIA DILDISGRIV LEIGPGEGIL TEALLERGAR VISVELDRTL
     IERLSRRFAS EIADGSLTLL QGDAVKVPLP PFEIVMANLP YSISSPITFR LLDIGFEAAI
     LMYQKEFADR MMAHPGTRDC GRLSIMLQTY ARANRCFDLP PGAFSPPPAV RSTVMWIEPR
     EPLFPIHDRK IYEDLVRELF TRRRKTVQST LKALAGMFGK EKIDSVVRDL NPEILSSRPE
     ALYLEDFATI SNQLSS