A0A164Q6L5 · A0A164Q6L5_9AGAM

Function

function

Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site.

165350100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site305ATP (UniProtKB | ChEBI)
Binding site354-361ATP (UniProtKB | ChEBI)
Binding site418-419ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentP-body
Cellular ComponentPAN complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionpoly(A) binding
Molecular Functionprotein kinase activity
Biological ProcessmRNA processing
Biological Processnuclear-transcribed mRNA poly(A) tail shortening

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    PAN2-PAN3 deadenylation complex subunit PAN3
  • Alternative names
    • PAB1P-dependent poly(A)-specific ribonuclease
    • Poly(A)-nuclease deadenylation complex subunit 3
      (PAN deadenylation complex subunit 3
      )

Gene names

    • Name
      PAN3
    • ORF names
      SISNIDRAFT_458877

Organism names

  • Taxonomic identifier
  • Strain
    • HHB9708
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Trechisporales > Trechisporales incertae sedis > Sistotremastrum

Accessions

  • Primary accession
    A0A164Q6L5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain), conferring substrate specificity of the enzyme complex.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain, zinc finger, coiled coil.

Type
IDPosition(s)Description
Region22-49Disordered
Compositional bias24-43Polar residues
Domain48-77C3H1-type
Zinc finger48-77C3H1-type
Region75-94Disordered
Compositional bias85-94Polar residues
Domain249-557Protein kinase
Coiled coil518-556
Region557-653Knob domain

Domain

Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.
The N-terminal zinc finger binds to poly(A) RNA.
The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.

Sequence similarities

Belongs to the protein kinase superfamily. PAN3 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    653
  • Mass (Da)
    73,131
  • Last updated
    2016-07-06 v1
  • MD5 Checksum
    598ACF8DB93E7AAC359A89497B63FA48
MDHTRAALSFPSRPSAAIKIVAPTTKSFSPTPSENGSASTSKSSPKKDFAQRQCRNVLIHGSCKLEGKGCVYYHPPREKTPQPPSFDSNSQTSPQLSVHVNAPVFVPKGSTFIDRGSPPKLSLNGGNTATPLQRPGSTASAATLVHNSEYDPYDPYDHSDAPVMPPQLMEGLHISQADFNSYAAPQGADYNGISAMDSYYSPHKTNFIRQPLNYHLYSNPIPPNPQASTARFFVSDSTREELQKRSETVYASVSLGTGVPEDVAGYHSLSPLEPTGGERRKSFGNWHSTVYRAIKATDGITYALRRVESFRLVQEAAFKSIDAWTRIRHPNIVAIREAFTTRSFNDSSLVVVYDFHPNASTLFDTHIRPKPLTYMNGRIQPQNAPIPERVIWTYLIQLANAIKTVHDAGLAIRTIDATKVLLTGKNRIRISSCGVWDVLSFEPRRDLHLLQLQQEDLLMFGRLMLSLCCQNLAAYNNFHKSMETMQRSYSSDLNNVILFLVSPGPPKEIGNLFNMIGSRLLTEMDSMQYRGDVLENELMAELENGRLVRLLCKFGFINERPEFDHEPRWSETGDRYIIRLFRDYVFHQVDENGNPVVNLSHVLTCLNKLDVGSDERIMLVSRDEQSCLVVSYKEIKSCISTAFSDLTRGSTRP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias24-43Polar residues
Compositional bias85-94Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV419428
EMBL· GenBank· DDBJ
KZS89375.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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