(data stored in ACNUC7421 zone)

SWISSPROT: RSMA_ECODH

ID   RSMA_ECODH              Reviewed;         273 AA.
AC   B1XC52;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 61.
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=ECDH10B_0052;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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: 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: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; CP000948; ACB01256.1; -; Genomic_DNA.
DR   RefSeq; WP_001065381.1; NC_010473.1.
DR   ProteinModelPortal; B1XC52; -.
DR   SMR; B1XC52; -.
DR   EnsemblBacteria; ACB01256; ACB01256; ECDH10B_0052.
DR   KEGG; ecd:ECDH10B_0052; -.
DR   eggNOG; ENOG4105D1X; Bacteria.
DR   eggNOG; COG0030; LUCA.
DR   HOGENOM; HOG000227962; -.
DR   KO; K02528; -.
DR   OMA; KRFGQHW; -.
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; B1XC52.
DR   SWISS-2DPAGE; B1XC52.
KW   Cytoplasm; Methyltransferase; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    273       Ribosomal RNA small subunit
FT                                methyltransferase A.
FT                                /FTId=PRO_1000130273.
FT   BINDING      18     18       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00607}.
FT   BINDING      20     20       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00607}.
FT   BINDING      45     45       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00607}.
FT   BINDING      66     66       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00607}.
FT   BINDING      91     91       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}.
SQ   SEQUENCE   273 AA;  30420 MW;  BBB163A0F4011C9D CRC64;
     MNNRVHQGHL ARKRFGQNFL NDQFVIDSIV SAINPQKGQA MVEIGPGLAA LTEPVGERLD
     QLTVIELDRD LAARLQTHPF LGPKLTIYQQ DAMTFNFGEL AEKMGQPLRV FGNLPYNIST
     PLMFHLFSYT DAIADMHFML QKEVVNRLVA GPNSKAYGRL SVMAQYYCNV IPVLEVPPSA
     FTPPPKVDSA VVRLVPHATM PHPVKDVRVL SRITTEAFNQ RRKTIRNSLG NLFSVEVLTG
     MGIDPAMRAE NISVAQYCQM ANYLAENAPL QES
//

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