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Database: UniProt
Entry: A0A1Q2SNM2_9GAMM
LinkDB: A0A1Q2SNM2_9GAMM
Original site: A0A1Q2SNM2_9GAMM 
ID   A0A1Q2SNM2_9GAMM        Unreviewed;       268 AA.
AC   A0A1Q2SNM2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=TAO_1366 {ECO:0000313|EMBL:BAW80736.1};
OS   Candidatus Nitrosoglobus terrae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Candidatus Nitrosoglobus.
OX   NCBI_TaxID=1630141 {ECO:0000313|EMBL:BAW80736.1, ECO:0000313|Proteomes:UP000243679};
RN   [1] {ECO:0000313|EMBL:BAW80736.1, ECO:0000313|Proteomes:UP000243679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAO100 {ECO:0000313|EMBL:BAW80736.1,
RC   ECO:0000313|Proteomes:UP000243679};
RX   PubMed=28072419; DOI=10.1038/ismej.2016.191;
RA   Hayatsu M., Tago K., Uchiyama I., Toyoda A., Wang Y., Shimomura Y.,
RA   Okubo T., Kurisu F., Hirono Y., Nonaka K., Akiyama H., Itoh T., Takami H.;
RT   "An acid-tolerant ammonia-oxidizing ?-proteobacterium from soil.";
RL   ISME J. 11:1130-1141(2017).
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}.
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DR   EMBL; AP014836; BAW80736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2SNM2; -.
DR   KEGG; ntt:TAO_1366; -.
DR   Proteomes; UP000243679; 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   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; 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_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; PS01131; RRNA_A_DIMETH; 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:UP000243679};
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          22..194
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         15
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         17
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         42
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         63
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         88
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         109
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   268 AA;  30490 MW;  B8EC4C5BD3733C4C CRC64;
     MMAREHQARK RFGQHFLHDS QIIERLMSTI NPQSGDLIVE IGPGQGALTF PLLKRLGYLE
     AIEIDRDLVA YLMGICAAKG DLRLHNTDAL AFNFHTIARK NQLLRVVGNL PYNISTPLLF
     HLFTQIEIIK DLHFMLQREV VMRMAAKPGN KNYGRLSVMT QFYCEVEPLF IVKPGAFIPP
     PKVDSMIVRL KPHHSPLAPD IPHKALSQVV SQAFSQRRKT LANSLKGLID LVAIKALGID
     PQQRPEIISL EQYLRLTQYW LAQDRNDL
//
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