Q9IA92 · Q9IA92_XENLA

Function

function

Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.

Catalytic activity

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site126Phosphocysteine intermediate
Active site295N6-GMP-lysine intermediate
Binding site300GTP (UniProtKB | ChEBI)
Binding site316GTP (UniProtKB | ChEBI)
Binding site344-346GTP (UniProtKB | ChEBI)
Binding site459-461GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionGTP binding
Molecular FunctionmRNA 5'-triphosphate monophosphatase activity
Molecular FunctionmRNA guanylyltransferase activity
Molecular Functionpolynucleotide 5'-phosphatase activity
Molecular Functionprotein tyrosine/serine/threonine phosphatase activity
Biological Process7-methylguanosine mRNA capping

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    mRNA-capping enzyme

Including 2 domains:

  • Recommended name
    mRNA 5'-triphosphate monophosphatase
  • EC number
  • Alternative names
    • mRNA 5'-phosphatase
  • Recommended name
    mRNA guanylyltransferase
  • EC number
  • Alternative names
    • GTP--RNA guanylyltransferase
      (GTase
      )

Gene names

    • Name
      xCAP1b

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    Q9IA92

Subcellular Location

Keywords

  • Cellular component

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-183Tyrosine-protein phosphatase
Domain104-171Tyrosine specific protein phosphatases

Sequence similarities

In the C-terminal section; belongs to the eukaryotic GTase family.
In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    511
  • Mass (Da)
    58,656
  • Last updated
    2000-10-01 v1
  • Checksum
    9860AF677D1EF85A
MAHNKIPPRWLNCPRRGQPVAAKFLPLKTMLGPKYDDQVPEENRFHPSMLSNYLKSLKVKMGLLVDLTNTTRFYDRNDIEKEGIKYIKLQCKGHGECPSQENTDTFLRLCDHFIDRNPTELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKADYLKELFRRYGDIEDAPKPPELPDWCFEEEDVDDEGNNVFQEAEAGSSGATYNRRKKERLKLGAIFLEGVTVKHVNQITTEPKLGEVQRKCQQFCSWRGSGFPGTQPVSMDKNNIKFMEQKSYKVSWKADGTRYMMIIDGKNQVFMIDRDNSVFHVTNLEFPFRKDLNQHLNNTLLDGEMIIDKVNGQVVPRYLIYDIIKFNGQPVGDCDFNIRLACIEKEIIFPRHEKMKTGLIDKAKEPFSVRSKPFFDIHAARKLLEGSFAREVSHEVDGLIFQPIGKYKAGRCDEILKWKPPNLNSVDFLLKITKVGGEGLLTRNVGLLYVGKYDCPFSEIKDLYLMGLL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF218794
EMBL· GenBank· DDBJ
AAF43144.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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