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MET16_DROME
ID   MET16_DROME             Reviewed;         305 AA.
AC   Q7K3B9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=CG7544;
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: 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; AE013599; AAF58169.2; -; Genomic_DNA.
DR   EMBL; AY058680; AAL13909.1; -; mRNA.
DR   RefSeq; NP_001163156.1; NM_001169685.2.
DR   RefSeq; NP_611015.1; NM_137171.4.
DR   AlphaFoldDB; Q7K3B9; -.
DR   SMR; Q7K3B9; -.
DR   BioGRID; 62420; 1.
DR   IntAct; Q7K3B9; 1.
DR   STRING; 7227.FBpp0086548; -.
DR   PaxDb; Q7K3B9; -.
DR   PRIDE; Q7K3B9; -.
DR   DNASU; 36680; -.
DR   EnsemblMetazoa; FBtr0087417; FBpp0086548; FBgn0033994.
DR   EnsemblMetazoa; FBtr0300324; FBpp0289552; FBgn0033994.
DR   GeneID; 36680; -.
DR   KEGG; dme:Dmel_CG7544; -.
DR   UCSC; CG7544-RA; d. melanogaster.
DR   FlyBase; FBgn0033994; CG7544.
DR   VEuPathDB; VectorBase:FBgn0033994; -.
DR   eggNOG; KOG2912; Eukaryota.
DR   GeneTree; ENSGT00390000016694; -.
DR   HOGENOM; CLU_027534_3_0_1; -.
DR   InParanoid; Q7K3B9; -.
DR   OMA; HQGRYDF; -.
DR   OrthoDB; 1358504at2759; -.
DR   PhylomeDB; Q7K3B9; -.
DR   BioGRID-ORCS; 36680; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 36680; -.
DR   PRO; PR:Q7K3B9; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033994; Expressed in ovary and 21 other tissues.
DR   ExpressionAtlas; Q7K3B9; baseline and differential.
DR   Genevisible; Q7K3B9; DM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0052907; F:23S rRNA (adenine(1618)-N(6))-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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   2: Evidence at transcript level;
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_0000310773"
FT   REGION          197..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q86W50"
SQ   SEQUENCE   305 AA;  35146 MW;  8C0045CFBCAA22EF CRC64;
     MVKTKGNQKI VGMHPRNVLR TQPDYTKMAI KYKDFRQQCQ LELNGKVSVN FRNEKTLREL
     TKMLLKEYYD LDVDFAPGSL VPTLALRLNY ILWLEDLMEP LNLQNIRGID IGCGSSCIYS
     LLGAKKNGWH MLALESKPQN IEYAKENVKR NHMESLIEVY AQPDNTNIFK SYFEQDQQQL
     QYQFCLCNPP FFDSNLPNPL GGNTRNPERR PAPNNARTGS QEELTCVGGE VQFVQRIIDE
     SLENKERVRI FTTMLGVKAN VPRILDYLKE LQVANVSTTE FHQGHTTRWA VAWSFHSEPL
     QQGTT
 
 
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