(data stored in ACNUC7421 zone)

SWISSPROT: DIM1_ASHGO

ID   DIM1_ASHGO              Reviewed;         319 AA.
AC   Q75C90;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 91.
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=ACR026W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016816; AAS51253.1; -; Genomic_DNA.
DR   RefSeq; NP_983429.1; NM_208782.1.
DR   SMR; Q75C90; -.
DR   STRING; 33169.AAS51253; -.
DR   PRIDE; Q75C90; -.
DR   EnsemblFungi; AAS51253; AAS51253; AGOS_ACR026W.
DR   GeneID; 4619554; -.
DR   KEGG; ago:AGOS_ACR026W; -.
DR   HOGENOM; HOG000227963; -.
DR   InParanoid; Q75C90; -.
DR   KO; K14191; -.
DR   OMA; VNAQMWA; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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.
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;
DR   PRODOM; Q75C90.
DR   SWISS-2DPAGE; Q75C90.
KW   Methyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..319
FT                   /note="Dimethyladenosine transferase"
FT                   /id="PRO_0000101458"
FT   BINDING         37
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         39
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         64
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         85
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         113
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         128
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   319 AA;  35818 MW;  13A921FF15E1D5C0 CRC64;
     MGKAAKKKYS GISTGKEVPS EQHMNTVFKF NTDLGQHILK NPLVAQGIVD KAQIKPSDIV
     LEVGPGTGNL TVRILEQARK VVAVEFDPRM AAELTKRVHG TPAEKKLEIM LGDFMKTELP
     YFDICISNTP YQISSPLVFK LINQPRPPRV SILMFQREFA MRLLARPGDS LYCRLSANVQ
     MWANVTHVMK VGRNNFRPPP QVESSVVRIE IKTPRPPVDF NEWDGLLRIV FVRKNRTISA
     GFKSTAVLEI MEKNYKAYLA TTNDAMVDDA KGSLAEQVKQ KIETVLAETG LSDKRAGKCD
     QTDFLKLLYA FHQVGLHFS
//

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