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Database: UniProt
Entry: A0A3Q9IBB1_9BACL
LinkDB: A0A3Q9IBB1_9BACL
Original site: A0A3Q9IBB1_9BACL 
ID   A0A3Q9IBB1_9BACL        Unreviewed;       288 AA.
AC   A0A3Q9IBB1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=rRNA adenine N-6-methyltransferase {ECO:0000256|ARBA:ARBA00016505};
DE   AltName: Full=Erythromycin resistance protein {ECO:0000256|ARBA:ARBA00030809};
DE   AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein {ECO:0000256|ARBA:ARBA00029941};
GN   Name=erm {ECO:0000313|EMBL:AZS16994.1};
GN   ORFNames=EI981_22720 {ECO:0000313|EMBL:AZS16994.1};
OS   Paenibacillus lutimineralis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2707005 {ECO:0000313|EMBL:AZS16994.1, ECO:0000313|Proteomes:UP000270678};
RN   [1] {ECO:0000313|Proteomes:UP000270678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBLB1234 {ECO:0000313|Proteomes:UP000270678};
RA   Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT   "Complete genome sequence of Paenibacillus sp. MBLB1234.";
RL   Submitted (DEC-2018) 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; CP034346; AZS16994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9IBB1; -.
DR   KEGG; plut:EI981_22720; -.
DR   OrthoDB; 9786598at2; -.
DR   Proteomes; UP000270678; 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; 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:UP000270678};
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          29..194
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         22
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         24
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         49
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   288 AA;  32741 MW;  E73C5C2AE06D9994 CRC64;
     MSENNKNRRE KWQKESNFSA QHLLISKRLI HDMIALAKIS PTDTVLDIGA GTGALTYPLA
     EKAAHVLAIE TDSAFVDRLF NKMKDRSNIR VKQSDFLEVS LPRSPFTVVA NIPYSITTPI
     MRKLLDHPGV PLQRAVLLVE KGAAKRFTAV PIIDPRILSW RMQYEIRLVR AVSPHHFAPP
     PKVDSAILFI QRREDPLVLT QHLPKFASLA AYGLRDPRLP LFAALSGVFT LPQIARLVRV
     LGVNREHPIG RLNEEQWGTV FDTMLQHVPP HRWPQWGKSS KGKFKRRK
//
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