ID A0A3L9Z129_9FLAO Unreviewed; 264 AA.
AC A0A3L9Z129;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, 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=rsmA {ECO:0000256|HAMAP-Rule:MF_00607};
GN Synonyms=ksgA {ECO:0000256|HAMAP-Rule:MF_00607};
GN ORFNames=BXY75_0633 {ECO:0000313|EMBL:RMA66214.1};
OS Ulvibacter antarcticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacter.
OX NCBI_TaxID=442714 {ECO:0000313|EMBL:RMA66214.1, ECO:0000313|Proteomes:UP000271339};
RN [1] {ECO:0000313|EMBL:RMA66214.1, ECO:0000313|Proteomes:UP000271339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23424 {ECO:0000313|EMBL:RMA66214.1,
RC ECO:0000313|Proteomes:UP000271339};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00607};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00607}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00607}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMA66214.1}.
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DR EMBL; REFC01000011; RMA66214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9Z129; -.
DR OrthoDB; 9814755at2; -.
DR Proteomes; UP000271339; Unassembled WGS sequence.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR011530; rRNA_adenine_dimethylase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00755; ksgA; 1.
DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00607};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00607}; Reference proteome {ECO:0000313|Proteomes:UP000271339};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00607};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00607};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00607};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00607}.
FT DOMAIN 21..191
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT BINDING 14
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 16
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 264 AA; 30125 MW; 4317135DF5D6ABD6 CRC64;
MSKEVRAKKH LGQHFLKDEH IAEKISDSLT LEGYNHVLEI GPGMGVLTKY LIEKDVEVIA
MDLDGESISY LSKTYHNKNL QLLEADFLRT DLKDVFGETS FAIIGNFPYN ISTQIVFKTL
ENKEQIPEFS GMFQKEVAKR ICASEGSKTY GILSVLTQAF YDAEYLFTVP PTVFSPPPKV
ESGVLRLRRK EDFSLPCSEK MLYKVVKTAF QQRRKTLRNS LKSFNLSEKI KEDTIFGQRP
EQLSVPQFIA LTLKLEEDAI STHE
//
