GenomeNet

Database: UniProt/TrEMBL
Entry: C7BKH3_PHOAA
LinkDB: C7BKH3_PHOAA
Original site: C7BKH3_PHOAA 
ID   C7BKH3_PHOAA            Unreviewed;       272 AA.
AC   C7BKH3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   11-JUN-2014, entry version 37.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase A;
DE            EC=2.1.1.182;
DE   AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase;
DE   AltName: Full=16S rRNA dimethyladenosine transferase;
DE   AltName: Full=16S rRNA dimethylase;
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase;
GN   Name=rsmA; Synonyms=ksgA; OrderedLocusNames=PAU_00567;
OS   Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 /
OS   3105-77) (Xenorhabdus luminescens (strain 2)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Photorhabdus.
OX   NCBI_TaxID=553480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43949 / 3105-77;
RX   PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA   Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA   Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA   Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA   Harris D., Thompson N.R., Quail M., Parkhill J.,
RA   ffrench-Constant R.H.;
RT   "Comparative genomics of the emerging human pathogen Photorhabdus
RT   asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL   BMC Genomics 10:302-302(2009).
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 (By similarity).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
CC       family. RsmA subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; FM162591; CAQ82659.1; -; Genomic_DNA.
DR   RefSeq; YP_003039404.1; NC_012962.1.
DR   STRING; 291112.PAU_00567; -.
DR   EnsemblBacteria; CAQ82659; CAQ82659; PAU_00567.
DR   GeneID; 13861020; -.
DR   KEGG; pay:PAU_00567; -.
DR   PATRIC; 20494723; VBIPhoAsy71438_0651.
DR   HOGENOM; HOG000227962; -.
DR   KO; K02528; -.
DR   OMA; DHVMVEI; -.
DR   OrthoDB; EOG66F08Z; -.
DR   BioCyc; PASY291112:GJQ0-584-MONOMER; -.
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   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR001737; rRNA_Ade_methylase_transferase.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   BINDING      18     18       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity){EA2}.
FT   BINDING      20     20       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity){EA2}.
FT   BINDING      45     45       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity){EA2}.
FT   BINDING      66     66       S-adenosyl-L-methionine (By
FT                                similarity){EA2}.
FT   BINDING      91     91       S-adenosyl-L-methionine (By
FT                                similarity){EA2}.
FT   BINDING     113    113       S-adenosyl-L-methionine (By
FT                                similarity){EA2}.
SQ   SEQUENCE   272 AA;  30596 MW;  F680E56A249674FD CRC64;
     MNNRVHQGHF ARKRFGQNFL TDQFVIDSIV AAINPQPGQA VLEIGPGLGA LTEPVGERMD
     KMTVVELDRD LAARLQVHPQ LKDKLTIIQQ DAMTVNFGEL SQQRGLPLRV FGNLPYNIST
     PLMFHLFSYT DAIADMHFML QKEVVNRLVA GPGSKAFGRL SVMAQYYCQV IPVLEVPPTA
     FTPAPKVDSA VVRLIPHKSI PYPVKNIRML SRITTQAFNQ RRKTIRNSLG DLFTVEQLTE
     FGIDPSTRAE NISVEQYCKM ANYLSEQPEM QL
//
DBGET integrated database retrieval system