ID A0A137QUD2_9AGAR Unreviewed; 438 AA.
AC A0A137QUD2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN ORFNames=AN958_03487 {ECO:0000313|EMBL:KXN90833.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN90833.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN90833.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN90833.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial transcription factor that confers selective
CC promoter recognition on the core subunit of the yeast mitochondrial RNA
CC polymerase. Interacts with DNA in a non-specific manner.
CC {ECO:0000256|ARBA:ARBA00024915}.
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, ECO:0000256|RuleBase:RU362106}.
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; KQ962027; KXN90833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QUD2; -.
DR STRING; 1714833.A0A137QUD2; -.
DR OrthoDB; 1430311at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
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 InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR PANTHER; PTHR11727:SF17; DIMETHYLADENOSINE TRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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}; Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; rRNA processing {ECO:0000256|RuleBase:RU362106};
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 BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 438 AA; 50058 MW; 2129F9CC5DFA14CC CRC64;
MAFRAASLTK HARTFTTRLS SAQKFSPTPR RLRFFSSTPI HHISSYSNDP PPPPLNSLVA
DAIKADNDTW PKRVTIRHPN GDISDDFDYT VLPPRGRWGE VFPWSMETKS RFALMDAEVA
KLLAEAYVPE GSKDRIVVEA FPGPGVLTRA LLDLPKDRIK KLIVLEDYDR YYNYLQPLQA
MDPRVTVLPV SGYMWTTYEF IEQMGLLKDV KTVDWSEEHP NLTFIGQIPY KVHGEQLVSQ
LFRSIPDQTW FFKYGRVPMH MILSECGILQ RISAPPGNNV VRCKLSVIAQ ATASLEQSIP
PEELTPYEEV FHPIHRRDST SLDFLSVTIT PLQEQLIQKG LMDDWDYCLR RLFVQKAQPI
KNSIVQLAPG AGSLLKKITS EDLPPRQRIS PKTPVRKLTV KEWKLLVETF ADWPFKPDDL
SIDSFHVSAT RQESKKVI
//
