A0A484CL50 · A0A484CL50_PERFV

Function

function

Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include ago2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by ago2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Endonucleolytic cleavage to 5'-phosphomonoester.
    EC:3.1.26.n2 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site608a divalent metal cation (UniProtKB | ChEBI)
Binding site680a divalent metal cation (UniProtKB | ChEBI)
Binding site820a divalent metal cation (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentP-body
Cellular ComponentRISC complex
Molecular Functionendoribonuclease activity, cleaving siRNA-paired mRNA
Molecular Functionmetal ion binding
Molecular FunctionmiRNA binding
Molecular FunctionmRNA cap binding
Molecular FunctionRNA 7-methylguanosine cap binding
Molecular Functionsingle-stranded RNA binding
Molecular FunctionsiRNA binding
Biological ProcessmiRNA-mediated gene silencing by inhibition of translation
Biological ProcessmiRNA-mediated gene silencing by mRNA destabilization
Biological Processnegative regulation of translational initiation
Biological Processpre-miRNA processing
Biological Processregulation of DNA-templated transcription

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein argonaute-2
  • EC number
  • Short names
    Argonaute2
  • Alternative names
    • Eukaryotic translation initiation factor 2C 2
      (eIF-2C 2
      ; eIF2C 2
      )
    • Protein slicer

Gene names

    • Name
      AGO2
    • Synonyms
      EIF2C2
    • ORF names
      EPR50_G00150330

Organism names

  • Taxonomic identifier
  • Strain
    • YP-PL-M2
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Percoidei > Percidae > Percinae > Perca

Accessions

  • Primary accession
    A0A484CL50

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of dicer1, ago2 and tarbp2. Note that the trimeric RLC/miRLC is also referred to as RISC.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-26Polar residues
Region1-39Disordered
Domain240-359PAZ
Domain528-831Piwi
Region835-856Disordered

Domain

The Piwi domain may perform RNA cleavage by a mechanism similar to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp-Glu (DDE) for metal ion coordination, this protein appears to utilize a triad of Asp-Asp-His (DDH).

Sequence similarities

Belongs to the argonaute family. Ago subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    872
  • Mass (Da)
    98,948
  • Last updated
    2019-06-05 v1
  • Checksum
    7635E3015518BEC7
MYSSAGVTEMQEGPRSSGSTGSDPPSSPVPEYVFKPPSRPDFGTMGRTIKLQANFFEMEIPKLEVYHYDIDIKPEKCPRRVNREIVEHMVQHFKTQIFGDRKPVYDGRKNLYTAMPLPIGRDKVELEVTIPGEGKDRSFKVSIKWMSCVSLQALHEALSGRLPSVPFETVQALDVVMRHLPSMRYTPVGRSFFTPSEGCSNPLGGGREVWFGFHQSVRPSLWKMMLNIDVSATAFYKAQPVIEFMCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQENGQTIECTVAQYFKDKYKLILRYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIRATARSAPDRQDEISKLMRSANFNTDPYVREFGVMVRDEMTEVNGRVLQAPSILYGGRNKAIATPIQGVWDMRNKQFHTGIEIKVWAIACFAPQRQCTELLLKAFTDQLRKISRDAGMPIQGQPCFCKYAQGADSVEPMFRHLKYTYQGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQVKNVQKTTPQTLSNLCLKINVKLGGVNNILLPQGRPLVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPSRYCATVRVQQHRQDIIQDLATMVRELLIQFYKSTRFKPTRIIYYRDGISEGQFNQMQVLQHELLAIREACIKLEKDYQPGITFVVVQKRHHTRLFCMDRNERVGKSGNIPAGTTVDTKITHPSEFDFYLCSHAGIQGTSRPSHYHVLWDDNHFSSDELQVLTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTSGQSNGRDQQALAKAVQIHQDTLRTMYFA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-26Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SCKG01000014
EMBL· GenBank· DDBJ
TDH04156.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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