HENMT_XENTR
ID HENMT_XENTR Reviewed; 369 AA.
AC C0IN03;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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;
DE AltName: Full=piRNA methyltransferase 1;
GN Name=henmt1; Synonyms=pimet1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Garcia M.A., Kidwell M.A., Heintzman S.E., Wormington M.;
RT "Activation of miRNA processing during Xenopus oocyte maturation.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; EU338244; ACA52291.1; -; mRNA.
DR RefSeq; NP_001153012.1; NM_001159540.1.
DR RefSeq; XP_012816150.1; XM_012960696.2.
DR RefSeq; XP_012816151.1; XM_012960697.2.
DR RefSeq; XP_012816152.1; XM_012960698.2.
DR AlphaFoldDB; C0IN03; -.
DR SMR; C0IN03; -.
DR STRING; 8364.ENSXETP00000013131; -.
DR PaxDb; C0IN03; -.
DR GeneID; 100286818; -.
DR KEGG; xtr:100286818; -.
DR CTD; 113802; -.
DR Xenbase; XB-GENE-998999; henmt1.
DR eggNOG; KOG1045; Eukaryota.
DR HOGENOM; CLU_044646_0_0_1; -.
DR InParanoid; C0IN03; -.
DR OMA; QRHQFVV; -.
DR OrthoDB; 789470at2759; -.
DR PhylomeDB; C0IN03; -.
DR TreeFam; TF315178; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000030501; Expressed in testis and 8 other tissues.
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; IEA:RHEA.
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..369
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000406961"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
SQ SEQUENCE 369 AA; 42977 MW; 3CAD9C57048A298F CRC64;
MELEFFKPPL YQQRYQFVKS YVDTYKPKKV ADLGCSTCSL LHTLRFWDCI KVLVGLDIDE
DVLSRKKFTL TPLPAHYLEP RNTSLTINLY QGSVTQKDPA LLGFDLITCI ELIEHLEAEE
LENFREVLFG FMAPITVIIS TPNAEFNILF PKCTGFRHPD HKFEWNRREF QSWATEVAKC
FNYTVEITGV GEPPRDSKNV GFCSQIAVFT RNYTESEESL QRKMECKSVY KTVLHIVYPS
LQEEKYLRRA VQKVALFHAY QIKANFLQQF IHREEEEEPH NTDTEHRPCM DLKLTSRWPT
LPQTEQDESM EPFLQEDTLY VPLKKIFSVP KVKELCGNMD NLRTMITGEA TLSNDGNAIL
YHIDLENSC
