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Database: UniProt
Entry: V5RWZ0_9BACT
LinkDB: V5RWZ0_9BACT
Original site: V5RWZ0_9BACT 
ID   V5RWZ0_9BACT            Unreviewed;       243 AA.
AC   V5RWZ0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Ribosomal RNA adenine methylase transferase N-terminal domain-containing protein {ECO:0000259|SMART:SM00650};
GN   ORFNames=RAAC3_TM7C00001G0614 {ECO:0000313|EMBL:AHB42460.1};
OS   Candidatus Saccharibacteria bacterium RAAC3_TM7_1.
OC   Bacteria; Candidatus Saccharibacteria.
OX   NCBI_TaxID=1394711 {ECO:0000313|EMBL:AHB42460.1, ECO:0000313|Proteomes:UP000018523};
RN   [1] {ECO:0000313|EMBL:AHB42460.1, ECO:0000313|Proteomes:UP000018523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAAC3_TM7_1 {ECO:0000313|EMBL:AHB42460.1,
RC   ECO:0000313|Proteomes:UP000018523};
RA   Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA   Castelle C.J., Thomas B.C., Banfield J.F.;
RT   "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT   four candidate phyla.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP006915; AHB42460.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5RWZ0; -.
DR   STRING; 1394711.RAAC3_TM7C00001G0614; -.
DR   KEGG; sbe:RAAC3_TM7C01G0614; -.
DR   HOGENOM; CLU_041220_3_0_0; -.
DR   BioCyc; CSAC1394711:G132K-614-MONOMER; -.
DR   Proteomes; UP000018523; Chromosome.
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; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000018523};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026};
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..183
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         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   243 AA;  27465 MW;  5ABD291E7582C16A CRC64;
     MARLHTYSQH FLKSPRLVAE LAGHSNIRKN DLVYDLGAGS GVISSALARR CKQVVAVEIE
     PLALEKLHKN VGNLQNVTIL KQDILTLNEP DGSYKIFANI PFSLSAEVIK KFTESPRPPK
     TMYLIVQKQF ARKLVPGDDH FTSLLSAQVG MRFVVRIRKP LNKTDFTPPP AVDTVLLELK
     LRDEPLVPSK ELESYRRYVE ECFSRQKYFA EQPLAAAGIS PELRPSQLTL EQWVALWTAK
     TKK
//
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