(data stored in ACNUC7421 zone)

SWISSPROT: RSMA_THEFY

ID   RSMA_THEFY              Reviewed;         287 AA.
AC   Q47SX4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 96.
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};
GN   OrderedLocusNames=Tfu_0405;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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:0000255|HAMAP-Rule:MF_00607}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-
CC         adenosyl-L-methionine = 4 H(+) + N(6)-
CC         dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA
CC         + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19609, Rhea:RHEA-
CC         COMP:10232, Rhea:RHEA-COMP:10233, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74493; EC=2.1.1.182; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00607};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00607}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
CC       family. RsmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00607}.
DR   EMBL; CP000088; AAZ54443.1; -; Genomic_DNA.
DR   RefSeq; WP_011290852.1; NC_007333.1.
DR   SMR; Q47SX4; -.
DR   STRING; 269800.Tfu_0405; -.
DR   EnsemblBacteria; AAZ54443; AAZ54443; Tfu_0405.
DR   KEGG; tfu:Tfu_0405; -.
DR   eggNOG; ENOG4105D1X; Bacteria.
DR   eggNOG; COG0030; LUCA.
DR   HOGENOM; HOG000227961; -.
DR   KO; K02528; -.
DR   OMA; KRFGQHW; -.
DR   OrthoDB; 2030110at2; -.
DR   BioCyc; TFUS269800:G1G4Q-410-MONOMER; -.
DR   Proteomes; UP000000434; 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   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;
DR   PRODOM; Q47SX4.
DR   SWISS-2DPAGE; Q47SX4.
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    287       Ribosomal RNA small subunit
FT                                methyltransferase A.
FT                                /FTId=PRO_0000257368.
FT   BINDING      35     35       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00607}.
FT   BINDING      37     37       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00607}.
FT   BINDING      62     62       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00607}.
FT   BINDING      83     83       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00607}.
FT   BINDING     113    113       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00607}.
FT   BINDING     131    131       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00607}.
SQ   SEQUENCE   287 AA;  30504 MW;  B84360A049AE86DA CRC64;
     MTESDSADAR LLTPADVRRL AAQLGIRPTK TLGQNFVIDP GTVRRIVRAA QVSPDDVVVE
     VGPGLGSLTL ALLPHVRHVT AVEIDPRLAE ALPGTVADHA PAYAHRLRVV TADALRITEL
     PDPQPTALVA NLPYNVAVPV VLHLLNLLPS LEHGLVMVQA EVAERLAARP GDRAYGAPSA
     KIAWYADVRR AGAIGRTVFW PVPNVDSGLV ALRRRPAPPT KASREDVFAV VDAAFAQRRK
     TLRAALSSWA GSAAAAEAAL RSAGVDPRSR GETLGIADFA RIAEHRP
//

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