ID O05649_STRVR Unreviewed; 259 AA.
AC O05649;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE SubName: Full=rRNA (Adenine-N6-)-methyltransferase {ECO:0000313|EMBL:AAB51440.1};
GN Name=ermSV {ECO:0000313|EMBL:AAB51440.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:AAB51440.1};
RN [1] {ECO:0000313|EMBL:AAB51440.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 2860 {ECO:0000313|EMBL:AAB51440.1};
RX PubMed=6163765;
RA Fujisawa Y., Weisblum B.;
RT "A family of r-determinants in Streptomyces spp. that specifies inducible
RT resistance to macrolide, lincosamide, and streptogramin type B
RT antibiotics.";
RL J. Bacteriol. 146:621-631(1981).
RN [2] {ECO:0000313|EMBL:AAB51440.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 2860 {ECO:0000313|EMBL:AAB51440.1};
RA Kamimiya S., Weisblum B.;
RL Submitted (MAY-1996) 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; U59450; AAB51440.1; -; Genomic_DNA.
DR RefSeq; WP_063844868.1; NG_047845.1.
DR AlphaFoldDB; O05649; -.
DR KEGG; ag:AAB51440; -.
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 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};
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 21..187
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT BINDING 14
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 16
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 259 AA; 28604 MW; 96566506D97B1664 CRC64;
MARPSRVSRA LSQNFLADRA AAGQLARLAA PHGLPVPLLL EVGAGKGALT ELLAPRCRSL
LAYEIDPRLV PVLRSRFADA PHVRVLGEDF LRARAPRTPF SVAGNVPFSR TAAVVAWCLR
APHLTDATLL TQLEYARRRT GDYGSWTRLT VLTWPRHEWR LAGRVGRRSF RPVPRVDAGI
VRIERRRTPL LAPGADAGWR ELVDLGFSGA GGSLHASLRR ARPRRRVDAA FRAAGLDRDV
LVGEVPPWTW LRLHEVLGS
//
