HENMT_BOMMO
ID HENMT_BOMMO Reviewed; 415 AA.
AC H9JDT2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 40.
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 Short=BmHen1 {ECO:0000303|PubMed:26919431};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [2]
RP FUNCTION.
RX PubMed=26919431; DOI=10.1016/j.cell.2016.01.008;
RA Izumi N., Shoji K., Sakaguchi Y., Honda S., Kirino Y., Suzuki T.,
RA Katsuma S., Tomari Y.;
RT "Identification and functional analysis of the pre-piRNA 3' trimmer in
RT silkworms.";
RL Cell 164:962-973(2016).
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:0000269|PubMed:26919431}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BABH01003003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BABH01003004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004928786.2; XM_004928729.2.
DR AlphaFoldDB; H9JDT2; -.
DR SMR; H9JDT2; -.
DR STRING; 7091.BGIBMGA007679-TA; -.
DR EnsemblMetazoa; BGIBMGA007679-RA; BGIBMGA007679-TA; BGIBMGA007679.
DR eggNOG; KOG1045; Eukaryota.
DR HOGENOM; CLU_044646_1_0_1; -.
DR InParanoid; H9JDT2; -.
DR OMA; LLEWNGY; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IMP: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 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..415
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000439353"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
SQ SEQUENCE 415 AA; 48476 MW; E80549019BEF81C0 CRC64;
MIIAIQTLIF FRQSLLTALD RLLRPYFQKF ALSLTKSSFE SDDDEPDENV FAEYDDEKGV
IFFPPMYVQR YAAIVDCLLD ERWSGKLDKV VDLGYHDMSF IKYLKEVSGI KSILGVDLET
IPLQCSSDLL SCNEYAPKRE TPLQISLLQG NAADPDYRLI GCDAVIAIEM IEHMLPHDLE
RLVHTVFAFI KPWIVIFTTP NDFKDVITGD INICKFNEKY LHRLNCTTLQ VKKFSKTTQG
LMAKNKVDAL VHTREVVEEI KHLTKMLNFN KSGLNQQDEK THIWYNFNWG ENAPYWNQYY
KIVREYNYPF ETKSDDCRIL DLISDEMNRL IDLQYDDILS VDLNKLEIPL QHLMQTVQHI
TDDVENVREL LEWNGYEVVD DMVIYSRLAI DNVTIDSQID DWQENESVSD VKKFN
