ID   A0A074RYX1_9AGAM        Unreviewed;       371 AA.
AC   A0A074RYX1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN   ORFNames=V565_048320 {ECO:0000313|EMBL:KEP52246.1};
OS   Rhizoctonia solani 123E.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP52246.1, ECO:0000313|Proteomes:UP000027456};
RN   [1] {ECO:0000313|EMBL:KEP52246.1, ECO:0000313|Proteomes:UP000027456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123E {ECO:0000313|EMBL:KEP52246.1,
RC   ECO:0000313|Proteomes:UP000027456};
RA   Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA   Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA   Zafar N., Nierman W.;
RL   Submitted (DEC-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEP52246.1}.
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DR   EMBL; AZST01000116; KEP52246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074RYX1; -.
DR   STRING; 1423351.A0A074RYX1; -.
DR   HOGENOM; CLU_034228_1_0_1; -.
DR   OrthoDB; 1430311at2759; -.
DR   Proteomes; UP000027456; 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:UP000027456};
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         13
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   371 AA;  41795 MW;  E54C1776A403C84B CRC64;
     MFNIPATKGR CSLIEPEVAR AFVRGALGLD EKLPKGSKKR KEGRVVIETF PGPGGVTRAL
     LELPRSEVKR VIVLEEELKF LPALKELEYY DDRVHVLSQS GFIWETYDIV KEMGLLDDVK
     VEDWKTAPHS TLSFVGHLPL GPVGEQLIAQ LLRAIPERSW LFKYGRMRMS WLLAQRMVER
     ITSPPPKAAR CKLTLIAEAT AKLTSALPQE ALADYDKYFW PKSESMVGGK KKTPLPRRIG
     QPFVAFNIDP QAEGSILSRE EAKEPQPQQI VATNKPITRV TLDKWDYVLR QLFILKSTPL
     EKAIQNLGPG ASILLSKLTG PGIPESRKVD IKAPINALSL QDFARIVEEF HKWPFAPDVL
     FIADQVEEER N
//