ID A0A2I1E2Y5_9GLOM Unreviewed; 319 AA.
AC A0A2I1E2Y5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN ORFNames=CHRIB12_LOCUS14781 {ECO:0000313|EMBL:CAB5375246.1},
GN RhiirA1_358327 {ECO:0000313|EMBL:PKC74676.1}, RhiirA4_540125
GN {ECO:0000313|EMBL:PKY42088.1}, RhiirA5_268600
GN {ECO:0000313|EMBL:PKC14611.1}, RhiirC2_758933
GN {ECO:0000313|EMBL:PKK62969.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKC74676.1, ECO:0000313|Proteomes:UP000232688};
RN [1] {ECO:0000313|Proteomes:UP000232722, ECO:0000313|Proteomes:UP000233469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY42088.1,
RC ECO:0000313|Proteomes:UP000234323}, A5 {ECO:0000313|EMBL:PKC14611.1,
RC ECO:0000313|Proteomes:UP000232722}, and C2
RC {ECO:0000313|EMBL:PKK62969.1, ECO:0000313|Proteomes:UP000233469};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKC14611.1, ECO:0000313|Proteomes:UP000232722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5 {ECO:0000313|EMBL:PKC14611.1,
RC ECO:0000313|Proteomes:UP000232722};
RA Chen E.C., Morin E., Beaudet D., Noel J., Ndikumana S., Charron P.,
RA St-Onge C., Giorgi J., Grigoriev I.V., Roux C., Martin F.M., Corradi N.;
RT "Extensive intraspecific genome diversity in a model arbuscular mycorrhizal
RT fungus.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000232688, ECO:0000313|Proteomes:UP000233469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:PKC74676.1,
RC ECO:0000313|Proteomes:UP000232688}, and C2
RC {ECO:0000313|EMBL:PKK62969.1, ECO:0000313|Proteomes:UP000233469};
RA Chen E.C.H., Morin E., Baudet D., Noel J., Ndikumana S., Charron P.,
RA St-Onge C., Giorgi J., Grigoriev I.V., Roux C., Martin F.M., Corradi N.;
RT "Extensive intraspecific genome diversity in a model arbuscular mycorrhizal
RT fungus.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PKC74676.1, ECO:0000313|Proteomes:UP000232688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:PKC74676.1,
RC ECO:0000313|Proteomes:UP000232688};
RA Corradi N., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAB5375246.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CHB12 {ECO:0000313|EMBL:CAB5375246.1};
RA Rincon C., Sanders R I., Robbins C., Chaturvedi A.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines in the loop
CC of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
CC {ECO:0000256|ARBA:ARBA00002977}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(1779)/adenosine(1780) in 18S rRNA + 4 S-adenosyl-L-
CC methionine = 4 H(+) + N(6)-dimethyladenosine(1779)/N(6)-
CC dimethyladenosine(1780) in 18S rRNA + 4 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42780, Rhea:RHEA-COMP:10234, Rhea:RHEA-COMP:10236,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.183;
CC Evidence={ECO:0000256|ARBA:ARBA00000248};
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:PKC74676.1}.
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DR EMBL; CAGKOT010000034; CAB5375246.1; -; Genomic_DNA.
DR EMBL; LLXJ01000126; PKC14611.1; -; Genomic_DNA.
DR EMBL; LLXH01000044; PKC74676.1; -; Genomic_DNA.
DR EMBL; LLXL01001761; PKK62969.1; -; Genomic_DNA.
DR EMBL; LLXI01000181; PKY42088.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FUN_001541; -.
DR VEuPathDB; FungiDB:GLOIN_2v1575080; -.
DR VEuPathDB; FungiDB:RhiirA1_358327; -.
DR OMA; GMFQKEV; -.
DR OrthoDB; 21458at2759; -.
DR Proteomes; UP000232688; Unassembled WGS sequence.
DR Proteomes; UP000232722; Unassembled WGS sequence.
DR Proteomes; UP000233469; Unassembled WGS sequence.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR Proteomes; UP000684084; Unassembled WGS sequence.
DR GO; GO:0052909; F:18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; 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; 1.
DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR InterPro; IPR001737; KsgA/Erm.
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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW 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 50..219
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 319 AA; 36040 MW; 3063DA57F6E38EAB CRC64;
MPKVKHQKFG YSHNSQSKNV TKSSTNTAAR SLAPLFNKDL GQHILKNPLV AQGIVEKAGL
KSTDTVLEVG PGTGNLTVRI LETAKKVVAV EMDPRLAAEL VKRVQGKPEQ KRLNIMVGDF
LKTELPYFDV CISNTPYQIS SPLIFKLLEH RPLFRCAILM FQREFAMRLI AKPGDNLYCR
LSINVQLYAK VDHIMKVGKN NFKPSPQVDS SVVRIEPYNP PPPISFKEWD GLMRIVFVRK
NKTLAANFKT TSVLQIIENN YKTFCSLNNM MIEDTLDIKQ KVINVLQSVD MAESRAAKLG
IDDFLKLLYA FNQANIHFC
//
