(data stored in SCRATCH3701 zone)

SWISSPROT: RSMA_LISMO

ID   RSMA_LISMO              Reviewed;         295 AA.
AC   Q8YAE2;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 100.
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=lmo0188;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
DR   EMBL; AL591973; CAC98403.1; -; Genomic_DNA.
DR   PIR; AE1098; AE1098.
DR   RefSeq; NP_463719.1; NC_003210.1.
DR   RefSeq; WP_003722718.1; NC_003210.1.
DR   SMR; Q8YAE2; -.
DR   STRING; 169963.lmo0188; -.
DR   PaxDb; Q8YAE2; -.
DR   EnsemblBacteria; CAC98403; CAC98403; CAC98403.
DR   GeneID; 39647233; -.
DR   GeneID; 987014; -.
DR   KEGG; lmo:lmo0188; -.
DR   PATRIC; fig|169963.11.peg.193; -.
DR   eggNOG; ENOG4105D1X; Bacteria.
DR   eggNOG; COG0030; LUCA.
DR   HOGENOM; HOG000227962; -.
DR   KO; K02528; -.
DR   OMA; YYIATRL; -.
DR   PhylomeDB; Q8YAE2; -.
DR   BioCyc; LMON169963:LMO0188-MONOMER; -.
DR   Proteomes; UP000000817; 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; IBA:GO_Central.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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; Q8YAE2.
DR   SWISS-2DPAGE; Q8YAE2.
KW   Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..295
FT                   /note="Ribosomal RNA small subunit methyltransferase A"
FT                   /id="PRO_0000101553"
FT   BINDING         29
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         31
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         56
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         77
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         102
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         128
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
SQ   SEQUENCE   295 AA;  33096 MW;  AAE0220F10AA8B80 CRC64;
     MSKDIATPGR TTEILKKYGF LFKKSLGQNF LIDSNILTRI TDTAEITKET NVIEIGPGIG
     ALTEQLAKTA NEVVAFEIDQ RLLPILDDTL SAYNNVKVVH GDVLKADVEE VIAEQFAKPE
     LPLKIVANLP YYVTTPIILK LLHDNIPADS MTFMLQKEVA DRISAVPSTK SYGSLTIAIQ
     FYMEAELAFI VPKTVFMPQP NVDSAVIHLK RRKEPLAEVN DEEFFFEVTR ASFAQRRKTL
     WNNLASKFPA LKPRKDELVE GLNAIGIDLI RRGETLDIPE FAKLSNFLGD FLKEK
//

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