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Small RNA 2'-O-methyltransferase (EC 2.1.1.n8) (HEN1 methyltransferase homolog 1)

 HENMT_DANRE             Reviewed;         402 AA.
Q568P9; Q5RH79;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
07-JUN-2017, entry version 64.
RecName: Full=Small RNA 2'-O-methyltransferase;
EC=2.1.1.n8 {ECO:0000269|PubMed:20859253};
AltName: Full=HEN1 methyltransferase homolog 1;
Name=henmt1; ORFNames=si:ch211-199m3.6, zgc:110175;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=20859253; DOI=10.1038/emboj.2010.233;
Kamminga L.M., Luteijn M.J., den Broeder M.J., Redl S., Kaaij L.J.,
Roovers E.F., Ladurner P., Berezikov E., Ketting R.F.;
"Hen1 is required for oocyte development and piRNA stability in
zebrafish.";
EMBO J. 29:3688-3700(2010).
-!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the
3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are
generated by a Dicer-independent mechanism and are primarily
derived from transposons and other repeated sequence elements.
This probably protects the 3'-end of piRNAs from uridylation and
adenylation activities and subsequent degradation. Stabilization
of piRNAs is essential for oocyte development.
{ECO:0000269|PubMed:20859253}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + small RNA = S-
adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-
methylnucleotide. {ECO:0000269|PubMed:20859253}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q9C5Q8};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20859253}.
Note=Component of the meiotic nuage, also named P granule, a germ-
cell-specific organelle required to repress transposon activity
during meiosis. {ECO:0000269|PubMed:20859253}.
-!- TISSUE SPECIFICITY: Gonad-specific. {ECO:0000269|PubMed:20859253}.
-!- DEVELOPMENTAL STAGE: Expression in gonads starts around 3 weeks of
age, which corresponds to the start of sex determination.
Expression remains present in the adult gonads, both in males and
females, although expression is weaker in testis.
{ECO:0000269|PubMed:20859253}.
-!- DISRUPTION PHENOTYPE: Defects in germ cell development due to
reduced piRNAs levels. {ECO:0000269|PubMed:20859253}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BX571790; CAI11740.1; -; Genomic_DNA.
EMBL; BC092772; AAH92772.1; -; mRNA.
RefSeq; NP_001017842.1; NM_001017842.2.
UniGene; Dr.36600; -.
ProteinModelPortal; Q568P9; -.
SMR; Q568P9; -.
STRING; 7955.ENSDARP00000004251; -.
PaxDb; Q568P9; -.
Ensembl; ENSDART00000015000; ENSDARP00000004251; ENSDARG00000018871.
GeneID; 550540; -.
KEGG; dre:550540; -.
CTD; 113802; -.
ZFIN; ZDB-GENE-050417-387; henmt1.
eggNOG; KOG1045; Eukaryota.
eggNOG; ENOG410XSD6; LUCA.
GeneTree; ENSGT00390000004798; -.
HOVERGEN; HBG097349; -.
InParanoid; Q568P9; -.
KO; K20798; -.
OMA; NSEFNPL; -.
OrthoDB; EOG091G08Y9; -.
PhylomeDB; Q568P9; -.
TreeFam; TF315178; -.
PRO; PR:Q568P9; -.
Proteomes; UP000000437; Chromosome 20.
Bgee; ENSDARG00000018871; -.
GO; GO:0043186; C:P granule; IDA:ZFIN.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0008173; F:RNA methyltransferase activity; IDA:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0048599; P:oocyte development; IMP:ZFIN.
GO; GO:0034587; P:piRNA metabolic process; IMP:ZFIN.
GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
InterPro; IPR026610; Hen1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR21404; PTHR21404; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Differentiation; Metal-binding;
Methyltransferase; Oogenesis; Reference proteome; RNA-binding;
RNA-mediated gene silencing; S-adenosyl-L-methionine; Transferase.
CHAIN 1 402 Small RNA 2'-O-methyltransferase.
/FTId=PRO_0000304143.
METAL 112 112 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 115 115 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 116 116 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 162 162 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
BINDING 58 58 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9C5Q8}.
BINDING 94 94 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9C5Q8}.
CONFLICT 161 161 D -> G (in Ref. 2; AAH92772).
{ECO:0000305}.
SEQUENCE 402 AA; 46124 MW; 6EA54C594C320690 CRC64;
MTATPFSPPL YMQRYQFVID YVKTYRPRKV IDFGCAECCL LKKLKFHRNG IQLLVGVDIN
SVVLLKRMHS LAPLVSDYLQ PSDGPLTIEL YQGSVMEREP CTKGFDLVTC VELIEHLELE
EVERFSEVVF GYMAPGAVIV TTPNAEFNPL LPGLRGFRNY DHKFEWTRAE FQTWAHRVCR
EHGYSVQFTG VGEAAGHWRD VGFCTQIAVF QRNFDGVNRS MSNAEHLEPS VYRLLYRVVY
PSLCDNNIYQ KTLINEVLYE AQHLRQQWLI RENMNNNAHF YSPPLMEALH HGAEGNACEQ
QPVYQQGGII CVPLARVWSC PRVQALCGSL QRLREKLLED ERVRMSADGS ALNLPADDDD
DNVEEEEEEE EEENQQNVKA VSGAVNNMEE DWDRELGSYG DE


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