ID   HENMT_RAT               Reviewed;         394 AA.
AC   Q32PY6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Small RNA 2'-O-methyltransferase;
DE            EC=2.1.1.n8 {ECO:0000250|UniProtKB:Q8CAE2};
DE   AltName: Full=HEN1 methyltransferase homolog 1;
GN   Name=Henmt1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end
CC       of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a
CC       Dicer-independent mechanism and are primarily derived from transposons
CC       and other repeated sequence elements. This probably protects the 3'-end
CC       of piRNAs from uridylation activity and subsequent degradation.
CC       Stabilization of piRNAs is essential for gametogenesis.
CC       {ECO:0000250|UniProtKB:Q8CAE2}.
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:0000250|UniProtKB:Q8CAE2};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9C5Q8};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}.
CC       Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC       specific organelle required to repress transposon activity during
CC       meiosis. {ECO:0000250|UniProtKB:Q568P9}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC       {ECO:0000305}.
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DR   EMBL; BC107926; AAI07927.1; -; mRNA.
DR   RefSeq; NP_001032744.2; NM_001037655.1.
DR   AlphaFoldDB; Q32PY6; -.
DR   SMR; Q32PY6; -.
DR   PaxDb; Q32PY6; -.
DR   GeneID; 100363095; -.
DR   KEGG; rno:100363095; -.
DR   CTD; 113802; -.
DR   RGD; 1306230; Henmt1.
DR   eggNOG; KOG1045; Eukaryota.
DR   InParanoid; Q32PY6; -.
DR   OrthoDB; 789470at2759; -.
DR   PhylomeDB; Q32PY6; -.
DR   PRO; PR:Q32PY6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008171; F:O-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008173; F:RNA methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; ISO:RGD.
DR   GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR   GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
DR   GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW   RNA-binding; RNA-mediated gene silencing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..394
FT                   /note="Small RNA 2'-O-methyltransferase"
FT                   /id="PRO_0000304142"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
SQ   SEQUENCE   394 AA;  45087 MW;  49926C2929EB43FD CRC64;
     METAENIPCS MLGDNFKEVC AEKVIRFRPP LYKQRYQFVR DLVDRHEPKK VADLGCGDTK
     LLKLLKIYPC IQLLVGVDIN EEKLHSNGHR LSPYLGEFVK PRDLDLTVTL YHGSVVERDS
     RLLGFDLITC IELIEHLDSD DLARFPEVVF GYLSPAMVVI STPNAEFNPL FPTVTLRDAD
     HKFEWSRMEF QTWASQVANC YNYCVEFTGV GTPPAGSEHV GYCTQIGVFR KNGGKLSEPS
     ASQQRDQHVY KAVYTTSYPS LQQEKVLKFV LVGELLIQVD RLRLRHQRML REQEKERGPK
     PWYTDSSPAP HLLLGAVFTE AEKARIENSP KPFCEGEKFY IPLQRLLTYP KLHRLCADED
     RMRSLIADSV CLSSDGSAVV VDLHNSWDYR PEDN