DIM1_BOVIN
ID DIM1_BOVIN Reviewed; 313 AA.
AC Q2KHT8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable dimethyladenosine transferase;
DE EC=2.1.1.183 {ECO:0000250|UniProtKB:Q9UNQ2};
DE AltName: Full=DIM1 dimethyladenosine transferase 1 homolog;
DE AltName: Full=DIM1 dimethyladenosine transferase 1-like;
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 Name=DIMT1; Synonyms=DIMT1L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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 Involved in the pre-rRNA processing steps leading to small-subunit rRNA
CC production independently of its RNA-modifying catalytic activity.
CC {ECO:0000250|UniProtKB:Q9UNQ2}.
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:0000250|UniProtKB:Q9UNQ2};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9UNQ2}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9UNQ2}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. {ECO:0000305}.
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DR EMBL; BC112886; AAI12887.1; -; mRNA.
DR RefSeq; NP_001039501.1; NM_001046036.2.
DR AlphaFoldDB; Q2KHT8; -.
DR SMR; Q2KHT8; -.
DR STRING; 9913.ENSBTAP00000015680; -.
DR PaxDb; Q2KHT8; -.
DR PRIDE; Q2KHT8; -.
DR Ensembl; ENSBTAT00000015680; ENSBTAP00000015680; ENSBTAG00000011812.
DR GeneID; 509725; -.
DR KEGG; bta:509725; -.
DR CTD; 27292; -.
DR VEuPathDB; HostDB:ENSBTAG00000011812; -.
DR VGNC; VGNC:28065; DIMT1.
DR eggNOG; KOG0820; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_041220_2_3_1; -.
DR InParanoid; Q2KHT8; -.
DR OMA; KEEEPYF; -.
DR OrthoDB; 963506at2759; -.
DR TreeFam; TF354255; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000011812; Expressed in oocyte and 106 other tissues.
DR ExpressionAtlas; Q2KHT8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 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 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 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..313
FT /note="Probable dimethyladenosine transferase"
FT /id="PRO_0000248512"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 35167 MW; 5FE3C4C9F9E3AB71 CRC64;
MPKIKSAASG RRRERQQQRG QLKSAGGLMF NTGIGQHILK NPLIVNSIID KAALRPTDVV
LEVGPGTGNM TVKLLEKAKK VIACELDPRL VAELHKRVQG TPLASKLQVM VGDVLKADLP
FFDACVANLP YQISSPFVFK LLLHRPFFRC AVLMFQREFA LRLVAKPGDK LYCRLSINTQ
LLARVDHLMK VGKNNFRPPP KVESSVVRIE PKNPPPPINF QEWDGLVRIT FVRKNKTLSA
AFKSSAVQQL LEKNYRIHCS VHNIIIPEDF SIADKIQQIL TSTGFSDKRA RSMDIDDFIR
LLHGFNAEGI HFS
