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Database: UniProt
Entry: A0A439D8U5_9PEZI
LinkDB: A0A439D8U5_9PEZI
Original site: A0A439D8U5_9PEZI 
ID   A0A439D8U5_9PEZI        Unreviewed;       354 AA.
AC   A0A439D8U5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN   ORFNames=EKO27_g4278 {ECO:0000313|EMBL:RWA10818.1};
OS   Xylaria grammica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX   NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA10818.1, ECO:0000313|Proteomes:UP000286045};
RN   [1] {ECO:0000313|EMBL:RWA10818.1, ECO:0000313|Proteomes:UP000286045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHI A82 {ECO:0000313|EMBL:RWA10818.1,
RC   ECO:0000313|Proteomes:UP000286045};
RA   Buettner E., Kellner H.;
RT   "Draft genome sequence of Xylaria grammica IHI A82.";
RL   Submitted (DEC-2018) 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, ECO:0000256|RuleBase:RU362106}.
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:RWA10818.1}.
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DR   EMBL; RYZI01000100; RWA10818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A439D8U5; -.
DR   STRING; 363999.A0A439D8U5; -.
DR   Proteomes; UP000286045; 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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.480; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000286045};
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   DOMAIN          46..195
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   354 AA;  39543 MW;  1FC2B1A803CD0FE9 CRC64;
     MGKAKTSKRN AGSGPYERPS KNNAATNNVF KFTKDLGQHI LRNPGIAQAI VDKAYLKPTD
     VVLEIGPGTG NLTVPILNQA KKVIAVEMDP RMAAEVTKRV QGKPEHKRLE VILGDVIKQD
     MTDVNFDVWA AEDLHFDVPK GIRAAAELHA LEILSMLSVN TQFWAKVSHV LKVGRANFRP
     PPKVDSDVVR IEPKVDRPNI SFEEFDGLLR IAFNRRNKVL RSLFLSNKEV LKLMESNYRL
     YCAQRDIPID EGLVEDAGED EEMEIDDNEH DASMDVDGDD DMPSFFGAAK NQDEGTPTGK
     KGSLKKTRLA VLVKEKVRKV LEETELAESR SAKMHENDFL RLLAAFNAEG IHFS
//
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