ID A0A143Y2Y5_9FIRM Unreviewed; 309 AA.
AC A0A143Y2Y5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=rRNA adenine N-6-methyltransferase {ECO:0000256|ARBA:ARBA00016505};
DE AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein {ECO:0000256|ARBA:ARBA00029941};
GN Name=ermD {ECO:0000313|EMBL:CVI73562.1};
GN ORFNames=BN3660_03162 {ECO:0000313|EMBL:CVI73562.1};
OS Eubacteriaceae bacterium CHKCI004.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=1780380 {ECO:0000313|EMBL:CVI73562.1, ECO:0000313|Proteomes:UP000199324};
RN [1] {ECO:0000313|EMBL:CVI73562.1, ECO:0000313|Proteomes:UP000199324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC4 {ECO:0000313|EMBL:CVI73562.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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; FCNR01000064; CVI73562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143Y2Y5; -.
DR SMR; A0A143Y2Y5; -.
DR STRING; 1780380.BN3660_03162; -.
DR OrthoDB; 9786598at2; -.
DR Proteomes; UP000199324; 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 CDD; cd00084; HMG-box_SF; 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:UP000199324};
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 16..183
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT REGION 276..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..293
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 11
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 309 AA; 35981 MW; 14CF5702848E9CD7 CRC64;
MKNLGYSQNF LVNKKLVERL ISKSNIDVTD YVIEIGPGKG IITDVLSQHA GEVVAVEYDQ
ELYNNLVRYH SHDNVTYIFG DFLKYKLPLN RRYKIFSNIP FQITADIIRK LTDDVNPPSD
INIIIQREAA KKNCGIPLQK YEGFRAAIIK AQYKVEITHS FKRSDFFPSP NVDTVMLHMQ
LWDDRLSGDD LQNYKDLVAF FYTNIKGETA KERLSILFSN EQIKRLGKAN RISLSNSYTL
ITAEQWMNIY YYSKIGLTDE KKKKFQDAYK KLQKMNKKLK KQNRTSLRKS SSNKKCRTRI
DTSNGTKNR
//
