DIM1_CAEEL
ID DIM1_CAEEL Reviewed; 308 AA.
AC Q09522;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable dimethyladenosine transferase;
DE EC=2.1.1.183;
DE AltName: Full=Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase;
DE AltName: Full=Probable 18S rRNA dimethylase;
DE AltName: Full=Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase;
GN ORFNames=E02H1.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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; Z47075; CAA87382.2; -; Genomic_DNA.
DR PIR; T20417; T20417.
DR RefSeq; NP_496061.2; NM_063660.7.
DR AlphaFoldDB; Q09522; -.
DR SMR; Q09522; -.
DR BioGRID; 48796; 2.
DR STRING; 6239.E02H1.1.1; -.
DR EPD; Q09522; -.
DR PaxDb; Q09522; -.
DR PeptideAtlas; Q09522; -.
DR EnsemblMetazoa; E02H1.1.1; E02H1.1.1; WBGene00008455.
DR GeneID; 183993; -.
DR KEGG; cel:CELE_E02H1.1; -.
DR UCSC; E02H1.1.1; c. elegans.
DR CTD; 183993; -.
DR WormBase; E02H1.1; CE30642; WBGene00008455; -.
DR eggNOG; KOG0820; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_041220_2_3_1; -.
DR InParanoid; Q09522; -.
DR OMA; KEEEPYF; -.
DR OrthoDB; 963506at2759; -.
DR PhylomeDB; Q09522; -.
DR PRO; PR:Q09522; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008455; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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; Nucleus; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..308
FT /note="Probable dimethyladenosine transferase"
FT /id="PRO_0000101468"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 308 AA; 34610 MW; 91AAD079D9F1F31C CRC64;
MGKTSKVKKT KAGSSTGNVQ SLPFNTDKGQ HILKNPGVVN AIVEKSALKA TDTVLEVGPG
TGNLTVKMLE VAKTVIACEI DPRMIAEVKK RVMGTPLQNK LQVNGGDVMK MEWPFFDVCV
ANLPYQISSP FVQKLLLHRP LPRYAVLMFQ KEFADRLVAR PGDKDYSRLS VNVQLLAKVE
MLMKVKRTEF RPPPKVDSAV VRIAPKNPPP PVNFVEWEGL LRLCFMRKNK TLMAIFRLSN
VIEVIEDNFR KVCSFKNKPI PKDLNMKKVI EETLTASGYG ESRARKMRVE DFLALLLAFN
KADIHFLS
