ID A0A099D5H5_9ACTN Unreviewed; 337 AA.
AC A0A099D5H5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=ErmE/ErmH/ErmO/ErmR family 23S rRNA (Adenine(2058)-N(6))-methyltransferase {ECO:0000313|EMBL:ASU79074.1};
DE SubName: Full=N-6-aminoadenine-N-methyltransferase {ECO:0000313|EMBL:AIS23774.1};
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:KGI81196.1};
GN Name=rsmA {ECO:0000313|EMBL:ASU79074.1};
GN Synonyms=ermE {ECO:0000313|EMBL:AIS23774.1};
GN ORFNames=CDG81_13135 {ECO:0000313|EMBL:ASU79074.1}, IL38_13240
GN {ECO:0000313|EMBL:KGI81196.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU79074.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:AIS23774.1, ECO:0000313|Proteomes:UP000029737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YIM90600 {ECO:0000313|EMBL:AIS23774.1,
RC ECO:0000313|Proteomes:UP000029737};
RX PubMed=25250723;
RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT "Identification and Characterization of a New Erythromycin Biosynthetic
RT Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT Producing Halophilic Actinomycete Isolated from Salt Field.";
RL PLoS ONE 9:E108129-E108129(2014).
RN [2] {ECO:0000313|EMBL:ASU79074.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU79074.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) 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; KJ143518; AIS23774.1; -; Genomic_DNA.
DR EMBL; CP022752; ASU79074.1; -; Genomic_DNA.
DR EMBL; JPMV01000021; KGI81196.1; -; Genomic_DNA.
DR RefSeq; WP_043573728.1; NZ_KN214176.1.
DR KEGG; aey:CDG81_13135; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_3_1_11; -.
DR OrthoDB; 3616874at2; -.
DR Proteomes; UP000029737; Unassembled WGS sequence.
DR Proteomes; UP000215043; Chromosome.
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 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; 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};
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 48..212
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
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 68
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 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 337 AA; 38518 MW; EA359650D0C08944 CRC64;
MSSSDESRPR RSQQERQHPK QNRPVLGRTE RDRNRRQFGQ NFLHDRKTLA RIAEVAELRP
DLPVLEVGPG KGLLTRKLAS RARQVTSYEI DSRLAKSLRE KLSEHRNIEV VNTDFLTTEP
PTEPFAFVGA IPYGITSAIV DWCLEAPTIE TATMVTQLEF ARKRTGDYGR WSRLTVMTWP
LFEWEFVEKV DRRLFRPVPK VDSAIIRLRR RSEPLLDGEA LERYKSMVEL GFTGVGGNIQ
ASLLRQYPKH RVAAALDHAS IGGGAVVAYI RPEQWLKLFE RLDRKEEPTR GRNQRGERTR
GGDHRVHGRG RRGPSEDGRS GGRSNGRSGR RGGPRQR
//
