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Database: UniProt
Entry: A0A0B9A5J3_BRELN
LinkDB: A0A0B9A5J3_BRELN
Original site: A0A0B9A5J3_BRELN 
ID   A0A0B9A5J3_BRELN        Unreviewed;       358 AA.
AC   A0A0B9A5J3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=rRNA (Adenine-N(6)-)-methyltransferase {ECO:0000313|EMBL:KHS50673.1};
DE            EC=2.1.1.181 {ECO:0000313|EMBL:KHS50673.1};
GN   ORFNames=AE0388_2745 {ECO:0000313|EMBL:KHS50673.1};
OS   Brevibacterium linens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS50673.1, ECO:0000313|Proteomes:UP000031488};
RN   [1] {ECO:0000313|EMBL:KHS50673.1, ECO:0000313|Proteomes:UP000031488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AE038-8 {ECO:0000313|EMBL:KHS50673.1,
RC   ECO:0000313|Proteomes:UP000031488};
RA   Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT   "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL   Submitted (NOV-2014) 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}.
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:KHS50673.1}.
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DR   EMBL; JTJZ01000022; KHS50673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B9A5J3; -.
DR   PATRIC; fig|1703.6.peg.2690; -.
DR   OrthoDB; 3616874at2; -.
DR   Proteomes; UP000031488; Unassembled WGS sequence.
DR   GO; GO:0052907; F:23S rRNA (adenine(1618)-N(6))-methyltransferase 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   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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000031488};
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          18..175
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   REGION          248..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         13
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         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   358 AA;  39922 MW;  3C145E092333EF09 CRC64;
     MHGGRHELGQ NFLRSSTTID TIASLARSTS GPIMEIGPGD GAVTAELYRL GRELTLVELD
     ETRLDHLEDT YPRAEVRHAD ILTTRLDRPV IVGNLPFHLT TPILRRLLRS GRWQRAILLT
     QWEVARKRAG IGGLTMMTAQ WAPWFDFRLV TRVPADAFAP KPSVDGGILT IDRCPTGSIP
     AKSRSEYQQF VRSVFTGRGR GMKGILSKMS ITDHRTLQST MDRNDIRGDT LPKDLTPDQW
     TGLFTELTTE TEQKNSGNHK TAKTTTQPKN AKKGQTMRNS KAPQQNPVTE AAPEKPLITG
     EMPIVGAQKA TEKLQASIPG ADPKAKSHDK GHLQAERGFM NQHQKPQQPQ PRWNLPRR
//
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