HENMT_MACFA
ID HENMT_MACFA Reviewed; 393 AA.
AC Q4R3W5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
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; ORFNames=QtsA-13748;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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; AB179150; BAE02201.1; -; mRNA.
DR RefSeq; NP_001271484.1; NM_001284555.1.
DR AlphaFoldDB; Q4R3W5; -.
DR SMR; Q4R3W5; -.
DR STRING; 9541.XP_005542587.1; -.
DR Ensembl; ENSMFAT00000009809; ENSMFAP00000035571; ENSMFAG00000002745.
DR GeneID; 102140180; -.
DR CTD; 113802; -.
DR VEuPathDB; HostDB:ENSMFAG00000002745; -.
DR eggNOG; KOG1045; Eukaryota.
DR GeneTree; ENSGT00390000004798; -.
DR OMA; QRHQFVV; -.
DR OrthoDB; 789470at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000002745; Expressed in temporal lobe and 4 other tissues.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; ISS: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 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..393
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000304140"
FT REGION 283..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
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 393 AA; 44573 MW; D21EE2C329A3A439 CRC64;
MEENNLQCSS VVDGNFEEVP RETAIQFKPP LYRQRYQFVK NLVDQHEPKK VADLGCGDTS
LLRLLKVNPC IELLVGVDIN EDKLRWRGDS LAPFMGDFLK PRDLNLTIIL YHGSVVERDS
RLLGFDLITC IELIEHLDSG DLARFPEVVF GYLSPSMIVI STPNSEFNPL FPSVTLRDSD
HKFEWTRMEF QTWALYVANR YDYSVEFTGV GEPPAGAENV GYCTQIGIFQ KNGGRATEAC
VSEQHDQHVY KAVFTTSYPS LQQERFFKLV LVNEVSQQVE SLRVSHLPRR KEQDGEQGDK
PKDIGGSKAP VPCFGPVFTE VEKAKIENSP KPFCVGDKFF VPLQRLLAYP RLNRLCANEE
MMRSVIADSI PLSSDGSAVV TDLCNYFDEQ FEF
