HENMT_DROME
ID HENMT_DROME Reviewed; 391 AA.
AC Q7K175;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Small RNA 2'-O-methyltransferase;
DE EC=2.1.1.n8;
DE AltName: Full=HEN1 methyltransferase homolog;
DE Short=DmHen1;
DE AltName: Full=piRNA methyltransferase;
GN Name=Hen1; Synonyms=Pimet; ORFNames=CG12367;
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).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17604629; DOI=10.1016/j.cub.2007.06.030;
RA Horwich M.D., Li C., Matranga C., Vagin V., Farley G., Wang P.,
RA Zamore P.D.;
RT "The Drosophila RNA methyltransferase, DmHen1, modifies germline piRNAs and
RT single-stranded siRNAs in RISC.";
RL Curr. Biol. 17:1265-1272(2007).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17606638; DOI=10.1101/gad.1563607;
RA Saito K., Sakaguchi Y., Suzuki T., Suzuki T., Siomi H., Siomi M.C.;
RT "Pimet, the Drosophila homolog of HEN1, mediates 2'-O-methylation of Piwi-
RT interacting RNAs at their 3' ends.";
RL Genes Dev. 21:1603-1608(2007).
RN [6]
RP FUNCTION.
RX PubMed=18463630; DOI=10.1038/nature07015;
RA Okamura K., Chung W.J., Ruby J.G., Guo H., Bartel D.P., Lai E.C.;
RT "The Drosophila hairpin RNA pathway generates endogenous short interfering
RT RNAs.";
RL Nature 453:803-806(2008).
RN [7]
RP FUNCTION.
RX PubMed=20558712; DOI=10.1126/science.1187058;
RA Ameres S.L., Horwich M.D., Hung J.H., Xu J., Ghildiyal M., Weng Z.,
RA Zamore P.D.;
RT "Target RNA-directed trimming and tailing of small silencing RNAs.";
RL Science 328:1534-1539(2010).
CC -!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end
CC of selected small RNAs. Mediates 2'-O-methylation of piRNAs, single-
CC stranded siRNAs and long hairpin RNA genes (hpRNAs). Methylation
CC protects the 3'-end of small RNAs from tailing and trimming and could
CC constitute a recognition signal for appropriate argonaute machineries.
CC {ECO:0000269|PubMed:17604629, ECO:0000269|PubMed:17606638,
CC ECO:0000269|PubMed:18463630, ECO:0000269|PubMed:20558712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) +
CC S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide;
CC Xref=Rhea:RHEA:37887, Rhea:RHEA-COMP:10415, Rhea:RHEA-COMP:10416,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:74898; EC=2.1.1.n8;
CC Evidence={ECO:0000269|PubMed:17604629, ECO:0000269|PubMed:17606638};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000305}.
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DR EMBL; AE013599; AAF58575.2; -; Genomic_DNA.
DR EMBL; AY069325; AAL39470.1; -; mRNA.
DR RefSeq; NP_610732.1; NM_136888.3.
DR AlphaFoldDB; Q7K175; -.
DR SMR; Q7K175; -.
DR BioGRID; 62083; 4.
DR STRING; 7227.FBpp0087092; -.
DR PaxDb; Q7K175; -.
DR PRIDE; Q7K175; -.
DR DNASU; 36301; -.
DR EnsemblMetazoa; FBtr0087984; FBpp0087092; FBgn0033686.
DR GeneID; 36301; -.
DR KEGG; dme:Dmel_CG12367; -.
DR UCSC; CG12367-RA; d. melanogaster.
DR CTD; 36301; -.
DR FlyBase; FBgn0033686; Hen1.
DR VEuPathDB; VectorBase:FBgn0033686; -.
DR eggNOG; KOG1045; Eukaryota.
DR GeneTree; ENSGT00390000004798; -.
DR HOGENOM; CLU_044646_1_0_1; -.
DR InParanoid; Q7K175; -.
DR OMA; YEQRYCA; -.
DR OrthoDB; 789470at2759; -.
DR PhylomeDB; Q7K175; -.
DR BioGRID-ORCS; 36301; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36301; -.
DR PRO; PR:Q7K175; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033686; Expressed in testis and 28 other tissues.
DR Genevisible; Q7K175; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; IDA:FlyBase.
DR GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IDA:FlyBase.
DR GO; GO:0030422; P:siRNA processing; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026610; Hen1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21404; PTHR21404; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..391
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000406963"
FT REGION 354..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 45570 MW; C0F5700DDEE5EF33 CRC64;
MFSHKFICGS LTKMTETGIT FDPPVYEQRY CATIQILEDA RWKDQIKKVV EFGCAEMRFF
QLMRRIETIE HIGLVDIDKS LLMRNLTSVN PLVSDYIRSR ASPLKVQILQ GNVADSSEEL
RDTDAVIAIE LIEHVYDDVL AKIPVNIFGF MQPKLVVFST PNSDFNVIFT RFNPLLPNGF
RHEDHKFEWS RDEFKNWCLG IVEKYPNYMF SLTGVGNPPK EYESVGPVSQ IAIFVRKDML
EMQLVNPLVS KPNIDKESIP YKLIHTVEYP FYVDTRTEKE KLWTEVQIEL QRFKRQFESS
EIEEGTYQDT CNMPIAFLLD RLEHVGATKE RIEELLLENN LTVENECVLI VSSDQESEWS
DPYKFSDRSS QDDALVDQEQ EEERWDQGPE S
