(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKJ5_PSEAB

ID   A0A0H2ZKJ5_PSEAB        Unreviewed;       268 AA.
AC   A0A0H2ZKJ5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000256|HAMAP-Rule:MF_00607};
DE            EC=2.1.1.182 {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethylase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
GN   Name=ksgA {ECO:0000256|HAMAP-Rule:MF_00607,
GN   ECO:0000313|EMBL:ABJ15556.1};
GN   Synonyms=rsmA {ECO:0000256|HAMAP-Rule:MF_00607};
GN   OrderedLocusNames=PA14_07730 {ECO:0000313|EMBL:ABJ15556.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15556.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15556.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15556.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_00607}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00633798}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
CC       family. RsmA subfamily. {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00633788}.
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DR   EMBL; CP000438; ABJ15556.1; -; Genomic_DNA.
DR   RefSeq; WP_003099569.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15556; ABJ15556; PA14_07730.
DR   KEGG; pau:PA14_07730; -.
DR   KO; K02528; -.
DR   OMA; KRFGQHW; -.
DR   Proteomes; UP000000653; 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-UniRule.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
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; A0A0H2ZKJ5.
DR   SWISS-2DPAGE; A0A0H2ZKJ5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00633772};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633775,
KW   ECO:0000313|EMBL:ABJ15556.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633771};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00644568};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633825};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633791,
KW   ECO:0000313|EMBL:ABJ15556.1}.
FT   DOMAIN       23    195       rADc. {ECO:0000259|SMART:SM00650}.
FT   BINDING      16     16       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      18     18       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00607, ECO:0000256|PROSITE-ProRule:
FT                                PRU01026}.
FT   BINDING      43     43       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      64     64       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      89     89       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING     110    110       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
SQ   SEQUENCE   268 AA;  30087 MW;  A16A96FF4341193A CRC64;
     MSELYQHRAR KRFGQNFLHD AGVIHRILRA IHAREGQRLL EIGPGQGALT EGLLGSGARL
     DVIELDQDLI PLLKLKFGLE SRFSLHQGDA LKFDFASLVE SGEKLRVVGN LPYNISTPLI
     FHLLEHAPVI EDMHFMLQKE VVERLAATPG GGDWGRLSIM VQYHCRVEHL FNVGPGAFNP
     PPKVDSAIVR LTPFAEPPHP ARDPKLLERV VREAFNQRRK TLRNTLKPLL SVEDIEAAEV
     DPTLRPEQLD LAAFVRLANR LAELPGNR
//

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