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Entry: A0A1F4XPJ5_9BACT
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Original site: A0A1F4XPJ5_9BACT 
ID   A0A1F4XPJ5_9BACT        Unreviewed;       215 AA.
AC   A0A1F4XPJ5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000313|EMBL:OGC83671.1};
DE   Flags: Fragment;
GN   ORFNames=A3D68_00650 {ECO:0000313|EMBL:OGC83671.1};
OS   Candidatus Adlerbacteria bacterium RIFCSPHIGHO2_02_FULL_52_17.
OC   Bacteria; Candidatus Adlerbacteria.
OX   NCBI_TaxID=1797240 {ECO:0000313|EMBL:OGC83671.1, ECO:0000313|Proteomes:UP000177564};
RN   [1] {ECO:0000313|EMBL:OGC83671.1, ECO:0000313|Proteomes:UP000177564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01026}.
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:OGC83671.1}.
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DR   EMBL; MEWU01000013; OGC83671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4XPJ5; -.
DR   STRING; 1797240.A3D68_00650; -.
DR   Proteomes; UP000177564; Unassembled WGS sequence.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01026};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}.
FT   DOMAIN          17..199
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         10
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         12
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         37
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         58
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|PROSITE-ProRule:PRU01026"
FT   BINDING         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   NON_TER         215
FT                   /evidence="ECO:0000313|EMBL:OGC83671.1"
SQ   SEQUENCE   215 AA;  23687 MW;  436609FBAD9E5C11 CRC64;
     MEKKKSLGQH FLYSKHYLAK IADAAELAAG DLVLEVGPGD GTLTRELLAH GTNVIAIEKD
     HRLIPLLRQT FAKEIASGKL RVVEGDILHF DISKCFPTVE SRESYKVVAN IPYYITGAIL
     EKFLSARHQP SSMTLLVQKE VAERITGHPS TSSGSPKESI LSLSVKVYGD PAYVCTVPRG
     AFAPPPDVDS AVLVIKNISR RHFSTEKQEE RFFAL
//
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