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Database: UniProt
Entry: Q6X0Q4_9LACO
LinkDB: Q6X0Q4_9LACO
Original site: Q6X0Q4_9LACO 
ID   Q6X0Q4_9LACO            Unreviewed;       245 AA.
AC   Q6X0Q4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=rRNA adenine N-6-methyltransferase {ECO:0000256|ARBA:ARBA00016505};
DE            EC=2.1.1.184 {ECO:0000256|ARBA:ARBA00012304};
DE   AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein {ECO:0000256|ARBA:ARBA00029941};
OS   Lactobacillus crispatus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=47770 {ECO:0000313|EMBL:AAQ01499.1};
RN   [1] {ECO:0000313|EMBL:AAQ01499.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CHCC3692 {ECO:0000313|EMBL:AAQ01499.1};
RX   PubMed=14660363; DOI=10.1128/AEM.69.12.7173-7180.2003;
RA   Stroman P., Muller C.C., Sorensen K.I.;
RT   "Heat shock treatment increases the frequency of loss of an erythromycin
RT   resistance-encoding transposable element from the chromosome of
RT   Lactobacillus crispatus CHCC3692.";
RL   Appl. Environ. Microbiol. 69:7173-7180(2003).
RN   [2] {ECO:0000313|EMBL:AAQ01499.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CHCC3692 {ECO:0000313|EMBL:AAQ01499.1};
RA   Stroeman P., Mueller C.C., Soerensen K.I.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(2085) in 23S rRNA + 2 S-adenosyl-L-methionine = 2
CC         H(+) + N(6)-dimethyladenosine(2085) in 23S rRNA + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42784, Rhea:RHEA-COMP:10237, Rhea:RHEA-
CC         COMP:10238, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.184;
CC         Evidence={ECO:0000256|ARBA:ARBA00001449};
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; AY262353; AAQ01499.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6X0Q4; -.
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};
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..179
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         100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   245 AA;  28794 MW;  A24D8E237329AC41 CRC64;
     MNKNIKYSQN FLTSEKVLNQ IIKQLNLKET DTVYEIGTGK GHLTTKLAKI SKQVTSIELD
     SHLFNLSSEK LKLNTRVTLI HQDILQFQFP NKQRYKIVGN IPYNLSTQII KKVVFESRAS
     DIYLIVEEGF YKRTLDIHRT LGLLLHTQVS IQQLLKLPAE CFHPKPKVNS VLIKLTRHTT
     DVPDKYWKLY TYFVSKWVNR EYRQLFTKNQ FHQAMKHAKV NNLSTITYEQ VLSIFNSYLL
     FNGRK
//
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