ID   MET16_DROPS             Reviewed;         305 AA.
AC   Q290Z2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase;
DE            EC=2.1.1.346 {ECO:0000250|UniProtKB:O42662, ECO:0000250|UniProtKB:Q86W50};
GN   ORFNames=GA20428;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: RNA N6-methyltransferase that mediates N6-methylation of
CC       adenine of U6 small nuclear RNA (U6 snRNA).
CC       {ECO:0000250|UniProtKB:O42662, ECO:0000250|UniProtKB:Q86W50}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-
CC         methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:52808, Rhea:RHEA-COMP:13573, Rhea:RHEA-COMP:13574,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.346;
CC         Evidence={ECO:0000250|UniProtKB:O42662,
CC         ECO:0000250|UniProtKB:Q86W50};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL16/RlmF
CC       family. {ECO:0000305}.
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DR   EMBL; CM000071; EAL25220.2; -; Genomic_DNA.
DR   RefSeq; XP_001360645.2; XM_001360608.3.
DR   AlphaFoldDB; Q290Z2; -.
DR   SMR; Q290Z2; -.
DR   STRING; 7237.FBpp0276765; -.
DR   EnsemblMetazoa; FBtr0278327; FBpp0276765; FBgn0080423.
DR   GeneID; 4804015; -.
DR   KEGG; dpo:Dpse_GA20428; -.
DR   eggNOG; KOG2912; Eukaryota.
DR   HOGENOM; CLU_027534_3_0_1; -.
DR   InParanoid; Q290Z2; -.
DR   OMA; HQGRYDF; -.
DR   Proteomes; UP000001819; Chromosome 3.
DR   Bgee; FBgn0080423; Expressed in female reproductive system and 2 other tissues.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProt.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR017182; METTL16/PsiM.
DR   InterPro; IPR010286; METTL16/RlmF.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13393; PTHR13393; 1.
DR   Pfam; PF05971; Methyltransf_10; 1.
DR   PIRSF; PIRSF037350; Mtase_ZK1128_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..305
FT                   /note="U6 small nuclear RNA (adenine-(43)-N(6))-
FT                   methyltransferase"
FT                   /id="PRO_0000310774"
FT   REGION          194..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         164
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
SQ   SEQUENCE   305 AA;  35174 MW;  5781F2591D5F9EEB CRC64;
     MVRNKKNKYA MHPRNILRVP PDYTKLAIKY RDFRQVCELE LTGKVSVNFR NEKTLRELSK
     MLLKEYFELD VDFAPGSLVP TLALRLNYIL WLEDMLLPLN LETVRGIDVG CGSSCIYSLL
     GAKKNGWNML ALESKEENID YARENVRRNN LEDLIEVYAQ PDKSNIFKSY FETEKLRKEF
     HFCLCNPPFF DSNSPNPFGG NTRNPQRRPA PNNVRTGSAE ELTCEGGEVH FVQRIIEESQ
     LNKQRVLIFT SMLGVKASVP KILDYLKERQ ITNVTTTEFH QGHTTRWAVA WSHQPTPLSP
     GTQCN