ID A8VEW4_9BACT Unreviewed; 213 AA.
AC A8VEW4;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 22-FEB-2023, entry version 44.
DE SubName: Full=ErmB {ECO:0000313|EMBL:ABW95853.1};
DE Flags: Fragment;
GN Name=ermB {ECO:0000313|EMBL:ABW95853.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:ABW95853.1};
RN [1] {ECO:0000313|EMBL:ABW95853.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19924466; DOI=10.1007/s00248-009-9610-0;
RA Koike S., Aminov R.I., Yannarell A.C., Gans H.D., Krapac I.G.,
RA Chee-Sanford J.C., Mackie R.I.;
RT "Molecular ecology of macrolide-lincosamide-streptogramin B methylases in
RT waste lagoons and subsurface waters associated with swine production.";
RL Microb. Ecol. 59:487-498(2010).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01026}.
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DR EMBL; EU168274; ABW95853.1; -; Genomic_DNA.
DR EMBL; EU168278; ABW95857.1; -; Genomic_DNA.
DR EMBL; EU168287; ABW95865.1; -; Genomic_DNA.
DR EMBL; EU168290; ABW95868.1; -; Genomic_DNA.
DR EMBL; EU168301; ABW95878.1; -; Genomic_DNA.
DR EMBL; EU168314; ABW95891.1; -; Genomic_DNA.
DR AlphaFoldDB; A8VEW4; -.
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 3..165
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABW95853.1"
FT NON_TER 213
FT /evidence="ECO:0000313|EMBL:ABW95853.1"
SQ SEQUENCE 213 AA; 24927 MW; 3A5806BE681452AC CRC64;
EKVLNQIIKQ LNLKETDTVY EIGTGKGHLT TKLAKISKQV TSIELDSHLF NLSSEKLKLN
TRVTLIHQDI LQFQFPNKQR YKIVGSIPYH LSTQIIKKVV FESHASDIYL IVEEGFYKRT
LDIHRTLGLL LHTQVSIQQL LKLPAECFHP KPKVNSVLIK LTRHTTDVPD KYWKLYTYFV
SKWVNREYRQ LFTKNQFHQA MKHAKVNNLS TIT
//
