DIM1_CANGA
ID DIM1_CANGA Reviewed; 317 AA.
AC Q6FKY3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Dimethyladenosine transferase;
DE EC=2.1.1.183;
DE AltName: Full=18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase;
DE AltName: Full=18S rRNA dimethylase;
DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase;
GN Name=DIM1; OrderedLocusNames=CAGL0L07678g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- 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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR EMBL; CR380958; CAG62081.1; -; Genomic_DNA.
DR RefSeq; XP_449111.1; XM_449111.1.
DR AlphaFoldDB; Q6FKY3; -.
DR SMR; Q6FKY3; -.
DR STRING; 5478.XP_449111.1; -.
DR EnsemblFungi; CAG62081; CAG62081; CAGL0L07678g.
DR GeneID; 2891000; -.
DR KEGG; cgr:CAGL0L07678g; -.
DR CGD; CAL0135164; CAGL0L07678g.
DR VEuPathDB; FungiDB:CAGL0L07678g; -.
DR eggNOG; KOG0820; Eukaryota.
DR HOGENOM; CLU_041220_2_0_1; -.
DR InParanoid; Q6FKY3; -.
DR OMA; VNAQMWA; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:EnsemblFungi.
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-KW.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR Gene3D; 3.40.50.150; -; 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 PANTHER; PTHR11727; PTHR11727; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00755; ksgA; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..317
FT /note="Dimethyladenosine transferase"
FT /id="PRO_0000101459"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 317 AA; 35920 MW; E15FB1EB6DCE4C02 CRC64;
MAKADKKKYS GATTNKQVAA EKHLTSVFKF NTDLGQHILK NPLVAQGIVD KAQIKPSDIV
LEVGPGTGNL TVRILEQARK VVAVEMDPRM AAELTKRVHG TPAEKKLEIM LGDFMKTELP
YFDICISNTP YQISSPLVFK LINQPRPPRV SILMFQREFA MRLLARPGDS LYCRLSANVQ
MWANVTHIMK VGRNNFRPPP QVESSVVRIE IKNPRPQIDF NEWDGLLRIV FVRKNRTISA
GFKSTTVLEI LEKNYKTFLA INNQSIDETE NLQSLIKQKI ETVLKETGLA EKRAGKCDQT
DFLKLLYAFH QVGIHFS
