(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHJ3_GEOS0

ID   A0A0F6BHJ3_GEOS0        Unreviewed;       295 AA.
AC   A0A0F6BHJ3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 26.
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=rsmA {ECO:0000256|HAMAP-Rule:MF_00607};
GN   Synonyms=ksgA {ECO:0000256|HAMAP-Rule:MF_00607};
GN   OrderedLocusNames=GY4MC1_0038 {ECO:0000313|EMBL:ADP72894.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72894.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72894.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72894.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:
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:0000256|HAMAP-
CC         Rule:MF_00607};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00344807}.
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:SAAS00540765}.
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DR   EMBL; CP002293; ADP72894.1; -; Genomic_DNA.
DR   RefSeq; WP_003247403.1; NC_014650.1.
DR   EnsemblBacteria; ADP72894; ADP72894; GY4MC1_0038.
DR   KEGG; gmc:GY4MC1_0038; -.
DR   KO; K02528; -.
DR   OMA; KRFGQHW; -.
DR   OrthoDB; 2030110at2; -.
DR   BioCyc; GSP581103:G1GOQ-49-MONOMER; -.
DR   Proteomes; UP000002034; 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; A0A0F6BHJ3.
DR   SWISS-2DPAGE; A0A0F6BHJ3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00423242};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314909};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314905};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00445489};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00423218};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314911,
KW   ECO:0000313|EMBL:ADP72894.1}.
FT   DOMAIN       38    214       rADc. {ECO:0000259|SMART:SM00650}.
FT   BINDING      31     31       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      33     33       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00607, ECO:0000256|PROSITE-ProRule:
FT                                PRU01026}.
FT   BINDING      58     58       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      79     79       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING     104    104       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING     129    129       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
SQ   SEQUENCE   295 AA;  33250 MW;  F84C455B5A7D5E02 CRC64;
     MNTNKDIATP GRTREILEKY GFSFKKSLGQ NFLIDTNILR KIVDVAGLSR ETGAIEIGPG
     IGALTEQLAR RAKKVVAFEI DQRLLPILED TLSPYENVRI IHQDVLKADI HRVIAEEFTD
     AADIMVVANL PYYVTTPIIM KLLTDNLPIR GIVVMLQKEV ADRISAQPGT KDYGSLSIAI
     QYYTEAEKIM TVPRTVFIPQ PNVDSAVIRL IKRKQPPVDV DDESFFFQVV RASFAQRRKT
     ILNNLISNLP NGKARKEKIE RILTENGIDP RRRGETLTME EFAALSNALR EVMCI
//

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