Q7K175 (HENMT_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Small RNA 2'-O-methyltransferase
EC=2.1.1.n8

Alternative name(s):
HEN1 methyltransferase homolog
Short name=DmHen1
piRNA methyltransferase

Gene names

Name:	Hen1
Synonyms:	Pimet
ORF Names:	CG12367

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methyltransferase that adds a 2'-O-methyl group at the 3'-end of selected small RNAs. Mediates 2'-O-methylation of piRNAs, single-stranded siRNAs and long hairpin RNA genes (hpRNAs). Methylation protects the 3'-end of small RNAs from tailing and trimming and could constitute a recognition signal for appropriate argonaute machineries. Ref.4 Ref.5 Ref.6 Ref.7
Catalytic activity	S-adenosyl-L-methionine + small RNA = S-adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-methylnucleotide. Ref.4 Ref.5
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Sequence similarities	Belongs to the methyltransferase superfamily. HEN1 family.

Ontologies

Keywords
Biological process	RNA-mediated gene silencing
Ligand	Metal-binding RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA methylation Inferred from direct assay Ref.4Ref.5. Source: FlyBase piRNA metabolic process Inferred from direct assay Ref.4. Source: UniProtKB production of siRNA involved in RNA interference Inferred from direct assay Ref.4. Source: UniProtKB
Molecular function	O-methyltransferase activity Inferred from direct assay Ref.4Ref.5. Source: FlyBase RNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 391	391	Small RNA 2'-O-methyltransferase		PRO_0000406963
Sites
	Metal binding	130	1	Magnesium By similarity
	Metal binding	133	1	Magnesium By similarity
	Metal binding	134	1	Magnesium; via tele nitrogen By similarity
	Metal binding	185	1	Magnesium; via tele nitrogen By similarity
	Binding site	76	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7K175 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: C0F5700DDEE5EF33	FASTA	391	45,570
	10 20 30 40 50 60 MFSHKFICGS LTKMTETGIT FDPPVYEQRY CATIQILEDA RWKDQIKKVV EFGCAEMRFF 70 80 90 100 110 120 QLMRRIETIE HIGLVDIDKS LLMRNLTSVN PLVSDYIRSR ASPLKVQILQ GNVADSSEEL 130 140 150 160 170 180 RDTDAVIAIE LIEHVYDDVL AKIPVNIFGF MQPKLVVFST PNSDFNVIFT RFNPLLPNGF 190 200 210 220 230 240 RHEDHKFEWS RDEFKNWCLG IVEKYPNYMF SLTGVGNPPK EYESVGPVSQ IAIFVRKDML 250 260 270 280 290 300 EMQLVNPLVS KPNIDKESIP YKLIHTVEYP FYVDTRTEKE KLWTEVQIEL QRFKRQFESS 310 320 330 340 350 360 EIEEGTYQDT CNMPIAFLLD RLEHVGATKE RIEELLLENN LTVENECVLI VSSDQESEWS 370 380 390 DPYKFSDRSS QDDALVDQEQ EEERWDQGPE S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"The Drosophila RNA methyltransferase, DmHen1, modifies germline piRNAs and single-stranded siRNAs in RISC." Horwich M.D., Li C., Matranga C., Vagin V., Farley G., Wang P., Zamore P.D. Curr. Biol. 17:1265-1272(2007) [PubMed: 17604629] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[5]	"Pimet, the Drosophila homolog of HEN1, mediates 2'-O-methylation of Piwi-interacting RNAs at their 3' ends." Saito K., Sakaguchi Y., Suzuki T., Suzuki T., Siomi H., Siomi M.C. Genes Dev. 21:1603-1608(2007) [PubMed: 17606638] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[6]	"The Drosophila hairpin RNA pathway generates endogenous short interfering RNAs." Okamura K., Chung W.J., Ruby J.G., Guo H., Bartel D.P., Lai E.C. Nature 453:803-806(2008) [PubMed: 18463630] [Abstract] Cited for: FUNCTION.
[7]	"Target RNA-directed trimming and tailing of small silencing RNAs." Ameres S.L., Horwich M.D., Hung J.H., Xu J., Ghildiyal M., Weng Z., Zamore P.D. Science 328:1534-1539(2010) [PubMed: 20558712] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAF58575.2. AY069325 mRNA. Translation: AAL39470.1.
RefSeq	NP_610732.1. NM_136888.2.
UniGene	Dm.573.
3D structure databases
ProteinModelPortal	Q7K175.
SMR	Q7K175. Positions 2-266.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7K175.
Proteomic databases
PRIDE	Q7K175.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0087984; FBpp0087092; FBgn0033686.
GeneID	36301.
KEGG	dme:Dmel_CG12367.
NMPDR	fig|7227.3.peg.4755.
UCSC	CG12367-RA. d. melanogaster.
Organism-specific databases
CTD	36301.
FlyBase	FBgn0033686. Hen1.
Phylogenomic databases
eggNOG	inNOG09610.
GeneTree	EMGT00050000014980.
InParanoid	Q7K175.
OMA	KYPNYMF.
OrthoDB	EOG9J6RX8.
PhylomeDB	Q7K175.
Gene expression databases
ArrayExpress	Q7K175.
Bgee	Q7K175.
Family and domain databases
ProtoNet	Search...
Other
NextBio	797815.

Entry information

Entry name

HENMT_DROME

Accession

Primary (citable) accession number: Q7K175

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 5, 2011
Last sequence update:	October 3, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project