RSMA_AQUAE
ID RSMA_AQUAE Reviewed; 248 AA.
AC O67680;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607};
DE EC=2.1.1.182 {ECO:0000255|HAMAP-Rule:MF_00607};
DE AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {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}; OrderedLocusNames=aq_1816;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEXES WITH RNA AND
RP S-ADENOSYL-L-HOMOCYSTEINE, AND RNA-BINDING.
RX PubMed=19278652; DOI=10.1016/j.str.2009.01.010;
RA Tu C., Tropea J.E., Austin B.P., Court D.L., Waugh D.S., Ji X.;
RT "Structural basis for binding of RNA and cofactor by a KsgA
RT methyltransferase.";
RL Structure 17:374-385(2009).
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:0000255|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: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; AE000657; AAC07637.1; -; Genomic_DNA.
DR PIR; F70456; F70456.
DR RefSeq; NP_214246.1; NC_000918.1.
DR RefSeq; WP_010881183.1; NC_000918.1.
DR PDB; 3FTC; X-ray; 1.68 A; A=1-248.
DR PDB; 3FTD; X-ray; 1.44 A; A=1-248.
DR PDB; 3FTE; X-ray; 3.00 A; A=1-248.
DR PDB; 3FTF; X-ray; 2.80 A; A=1-248.
DR PDB; 3R9X; X-ray; 2.80 A; B=1-248.
DR PDBsum; 3FTC; -.
DR PDBsum; 3FTD; -.
DR PDBsum; 3FTE; -.
DR PDBsum; 3FTF; -.
DR PDBsum; 3R9X; -.
DR AlphaFoldDB; O67680; -.
DR SMR; O67680; -.
DR STRING; 224324.aq_1816; -.
DR PRIDE; O67680; -.
DR EnsemblBacteria; AAC07637; AAC07637; aq_1816.
DR KEGG; aae:aq_1816; -.
DR PATRIC; fig|224324.8.peg.1403; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_0_2_0; -.
DR InParanoid; O67680; -.
DR OMA; KEEEPYF; -.
DR OrthoDB; 2030110at2; -.
DR BRENDA; 2.1.1.182; 396.
DR EvolutionaryTrace; O67680; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..248
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_0000101474"
FT BINDING 11
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT SITE 105
FT /note="Interaction with RNA"
FT SITE 198
FT /note="Interaction with RNA"
FT SITE 202
FT /note="Interaction with RNA"
FT SITE 204
FT /note="Interaction with RNA"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:3FTF"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3FTD"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:3FTD"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3FTC"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3FTD"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:3FTD"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:3FTF"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3FTD"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:3FTD"
SQ SEQUENCE 248 AA; 28355 MW; 259FA7AA81786AF8 CRC64;
MVRLKKSFGQ HLLVSEGVLK KIAEELNIEE GNTVVEVGGG TGNLTKVLLQ HPLKKLYVIE
LDREMVENLK SIGDERLEVI NEDASKFPFC SLGKELKVVG NLPYNVASLI IENTVYNKDC
VPLAVFMVQK EVAEKLQGKK DTGWLSVFVR TFYDVNYVMT VPPRFFVPPP KVQSAVIKLV
KNEKFPVKDL KNYKKFLTKI FQNRRKVLRK KIPEELLKEA GINPDARVEQ LSLEDFFKLY
RLIEDSGE
