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DIM1_DROME
ID   DIM1_DROME              Reviewed;         306 AA.
AC   Q9VAQ5;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
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=CG11837;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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; AE014297; AAF56847.1; -; Genomic_DNA.
DR   EMBL; AY061429; AAL28977.1; -; mRNA.
DR   RefSeq; NP_651660.1; NM_143403.4.
DR   AlphaFoldDB; Q9VAQ5; -.
DR   SMR; Q9VAQ5; -.
DR   IntAct; Q9VAQ5; 5.
DR   STRING; 7227.FBpp0084729; -.
DR   PaxDb; Q9VAQ5; -.
DR   PRIDE; Q9VAQ5; -.
DR   DNASU; 43429; -.
DR   EnsemblMetazoa; FBtr0085360; FBpp0084729; FBgn0039627.
DR   GeneID; 43429; -.
DR   KEGG; dme:Dmel_CG11837; -.
DR   UCSC; CG11837-RA; d. melanogaster.
DR   FlyBase; FBgn0039627; CG11837.
DR   VEuPathDB; VectorBase:FBgn0039627; -.
DR   eggNOG; KOG0820; Eukaryota.
DR   GeneTree; ENSGT00950000183142; -.
DR   HOGENOM; CLU_041220_2_3_1; -.
DR   InParanoid; Q9VAQ5; -.
DR   OMA; KEEEPYF; -.
DR   OrthoDB; 963506at2759; -.
DR   PhylomeDB; Q9VAQ5; -.
DR   BioGRID-ORCS; 43429; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 43429; -.
DR   PRO; PR:Q9VAQ5; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0039627; Expressed in ovary and 21 other tissues.
DR   Genevisible; Q9VAQ5; DM.
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   2: Evidence at transcript level;
KW   Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..306
FT                   /note="Probable dimethyladenosine transferase"
FT                   /id="PRO_0000101469"
FT   BINDING         30
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         32
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         57
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   306 AA;  35048 MW;  CA091714E43A0AFA CRC64;
     MPKVTKEKKS RIHNDVQKQG IVFNKDFGQH ILKNPLVITT MLEKAALRAT DVVLEIGPGT
     GNMTVRMLER AKKVIACEID TRLAAELQKR VQATPLQPKL QVLIGDFLKA ELPFFDLCIA
     NVPYQISSPL IFKLLLHRPL FRCAVLMFQR EFAERLVAKP GDKLYCRLSI NTQLLARVDM
     LMKVGKNNFR PPPKVESSVV RLEPKNPPPP VNFTEWDGLT RIAFLRKNKT LAATFKVTSV
     LEMLEKNYKL YRSLRNEPIE DDFKMQDKVI SILEEQDMAA KRARSMDIDD FMRLLLAFNS
     AGIHFN
 
 
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