A3LNL5 · DXO_PICST

Function

function

Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity).
The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity).
Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (PubMed:26101253).
Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (By similarity).
Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity).
Stimulates exoribonuclease activity of Rat1, allowing it to degrade RNAs with stable secondary structure more effectively (By similarity).

Catalytic activity

Cofactor

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

Note: Divalent metal cation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site107-109substrate
Binding site179a divalent metal cation (UniProtKB | ChEBI)
Binding site228substrate
Binding site230a divalent metal cation (UniProtKB | ChEBI)
Binding site249a divalent metal cation (UniProtKB | ChEBI)
Binding site250a divalent metal cation (UniProtKB | ChEBI)
Binding site251substrate
Binding site275substrate

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionnuclease activity
Molecular Functionnucleotide binding
Molecular FunctionRNA binding
Biological ProcessmRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Decapping nuclease RAI1
  • EC number
  • Short names
    SsRai1
  • Alternative names
    • NAD-capped RNA hydrolase RAI1
      (DeNADding enzyme RAI1
      ) (EC:3.6.1.-
      ) . EC:3.6.1.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      RAI1
    • ORF names
      PICST_55876

Organism names

Accessions

  • Primary accession
    A3LNL5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004516961-396Decapping nuclease RAI1

Interaction

Subunit

Interacts with RAT1; the interaction is direct, stabilizes RAT1 protein structure and stimulates its exoribonuclease activity (By similarity).
The interaction also stimulates RAI1 pyrophosphohydrolase activity, probably by recruiting it to mRNA substrates (By similarity).

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the DXO/Dom3Z family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    396
  • Mass (Da)
    46,084
  • Last updated
    2007-07-24 v2
  • Checksum
    86FA8C46A0A96B86
MMKTLSLQSRAKTTALKQPKEIFAFARDIDGEFVYDQKIVKDENVSYYYLPDSKIDGSIDLQAGYAKFKKIPEEKNMSDMKCLLTALTKYEQEHNNGEKVNVDIITYRGLMTKLLALPYNLNDPVDLNVLAYDGQLFINSDEEIELARRKEEDEHKQQSMTPEKYDHMKRCEFSGYKFEAIATLPKPWADCSRQQIDKRGKKMVNNYEQYISVIKTGIGEAKMLLAGEVDCVWDYIPEDGKDVLSHYMELKTTRILESNGQVVNFEKKLFKTWAQCFLMGIRKVVYGFRDDSFFLRDVELYKTEEIPLLIKNNALTENKSGGKINCTTALKWYGAVIEWLLQEIPRDDTSKAYRVSFDPSTRTFTLRELMGNENSRLRNGEMLTSEFKQWRESIQK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000496
EMBL· GenBank· DDBJ
ABN64879.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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