Q32PY6

PR
Gene name
Henmt1
Protein name
Small RNA 2'-O-methyltransferase
Names
HEN1 methyltransferase homolog 1
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:100363095
EC number
2.1.1.386: Methyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

209-338 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q32PY6

Entry ID Method Resolution Chain Position Source
AF-Q32PY6-F1 Predicted AlphaFoldDB

No variants for Q32PY6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q32PY6

No associated diseases with Q32PY6

No regional properties for Q32PY6

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q32PY6

Functions

Description
EC Number 2.1.1.386 Methyltransferases
Subcellular Localization
  • Cytoplasm
  • Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
P granule A small cytoplasmic, non-membranous RNA/protein complex aggregate in the primordial germ cells of many higher eukaryotes.

5 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
O-methyltransferase activity Catalysis of the transfer of a methyl group to the oxygen atom of an acceptor molecule.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA methyltransferase activity Catalysis of the transfer of a methyl group from a donor to a nucleoside residue in an RNA molecule.
small RNA 2'-O-methyltransferase activity Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the oxygen atom of a nucleoside residue in a small RNA molecule. Reaction: S-adenosyl-L-methionine + small RNA <=> S-adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-methylnucleotide.

3 GO annotations of biological process

Name Definition
piRNA metabolic process The chemical reactions and pathways involving piRNAs, Piwi-associated RNAs, a class of 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
RNA methylation Posttranscriptional addition of a methyl group to either a nucleotide or 2'-O ribose in a polyribonucleotide. Usually uses S-adenosylmethionine as a cofactor.
siRNA processing A process leading to the generation of a functional small interfering RNA (siRNA). Includes the cleavage of double-stranded RNA to form small interfering RNA molecules (siRNAs) of 21-23 nucleotides. May also include amplification of the siRNA by RNA-directed RNA polymerase.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q7K175 Hen1 Small RNA 2'-O-methyltransferase Drosophila melanogaster (Fruit fly) PR
Q8CAE2 Henmt1 Small RNA 2'-O-methyltransferase Mus musculus (Mouse) PR
10 20 30 40 50 60
METAENIPCS MLGDNFKEVC AEKVIRFRPP LYKQRYQFVR DLVDRHEPKK VADLGCGDTK
70 80 90 100 110 120
LLKLLKIYPC IQLLVGVDIN EEKLHSNGHR LSPYLGEFVK PRDLDLTVTL YHGSVVERDS
130 140 150 160 170 180
RLLGFDLITC IELIEHLDSD DLARFPEVVF GYLSPAMVVI STPNAEFNPL FPTVTLRDAD
190 200 210 220 230 240
HKFEWSRMEF QTWASQVANC YNYCVEFTGV GTPPAGSEHV GYCTQIGVFR KNGGKLSEPS
250 260 270 280 290 300
ASQQRDQHVY KAVYTTSYPS LQQEKVLKFV LVGELLIQVD RLRLRHQRML REQEKERGPK
310 320 330 340 350 360
PWYTDSSPAP HLLLGAVFTE AEKARIENSP KPFCEGEKFY IPLQRLLTYP KLHRLCADED
370 380 390
RMRSLIADSV CLSSDGSAVV VDLHNSWDYR PEDN