ID Q8GDV8_HELMO Unreviewed; 283 AA.
AC Q8GDV8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 81.
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};
DE Flags: Fragment;
GN Name=rsmA {ECO:0000313|EMBL:MTV48444.1};
GN ORFNames=GJ688_05530 {ECO:0000313|EMBL:MTV48444.1};
OS Heliobacterium mobile (Heliobacillus mobilis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliobacterium.
OX NCBI_TaxID=28064 {ECO:0000313|EMBL:AAN87468.1};
RN [1] {ECO:0000313|EMBL:AAN87468.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12446909; DOI=10.1126/science.1075558;
RA Raymond J., Zhaxybayeva O., Gogarten J.P., Gerdes S.Y., Blankenship R.E.;
RT "Whole-genome analysis of photosynthetic prokaryotes.";
RL Science 298:1616-1620(2002).
RN [2] {ECO:0000313|EMBL:AAN87468.1}
RP NUCLEOTIDE SEQUENCE.
RA Liolios K.G., Chu L., Ostrovskaya O., Mendybaeva N., Koukharenko V.,
RA Gerdes S., Kyrpides N., Overbeek R.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MTV48444.1, ECO:0000313|Proteomes:UP000430670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6151 {ECO:0000313|EMBL:MTV48444.1,
RC ECO:0000313|Proteomes:UP000430670};
RA Kyndt J.A., Meyer T.E.;
RT "Whole-genome sequence of a the green, strictly anaerobic photosynthetic
RT bacterium Heliobacillus mobilis DSM 6151.";
RL Submitted (NOV-2019) 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; AY142864; AAN87468.1; -; Genomic_DNA.
DR EMBL; WNKU01000004; MTV48444.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GDV8; -.
DR OrthoDB; 9814755at2; -.
DR Proteomes; UP000430670; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 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; IPR011530; rRNA_adenine_dimethylase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00755; ksgA; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000430670};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; rRNA processing {ECO:0000256|ARBA:ARBA00022552};
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 30..208
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 25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT NON_TER 283
FT /evidence="ECO:0000313|EMBL:AAN87468.1"
SQ SEQUENCE 283 AA; 31515 MW; 763DE049C1515AE7 CRC64;
MSKELRQRIA QYGIRAKKGL GQNFLSDSEY VYRIVDAAEL SSGDVVVEIG PGPATLTPHL
AEAVGPEGKV LAIEVDESLR PLLMDLCREY PQVEILWQDA LKVDYDAVTA PYRGDKPFTL
VANLPYYITT PIMMGLLEGR FNLSHMVIMV QKEVADRMLA RAGTKDYGAL SVAVQYHCEV
KLVTKVPPGA FIPPPKVSSA VVRLNRRRQP PVHVFDEKAF FRVVRAAFNQ RRKTLLNALG
GLGLEMTKTE MSERLAQAGI DPGRRGETLN LDEFARVTDA LYR
//
