E1ZZH4 · E1ZZH4_CAMFO

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 site130Phosphocysteine intermediate
Active site299N6-GMP-lysine intermediate
Binding site304GTP (UniProtKB | ChEBI)
Binding site320GTP (UniProtKB | ChEBI)
Binding site348-350GTP (UniProtKB | ChEBI)
Binding site465-467GTP (UniProtKB | ChEBI)
Binding site536-541GTP (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

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

    • ORF names
      EAG_12506

Organism names

  • Taxonomic identifier
  • Strain
    • C129
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Formicinae > Camponotus

Accessions

  • Primary accession
    E1ZZH4

Proteomes

Subcellular Location

Keywords

  • Cellular component

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain39-187Tyrosine-protein phosphatase
Domain108-175Tyrosine specific protein phosphatases
Region207-233Disordered
Compositional bias213-233Basic and acidic residues

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    591
  • Mass (Da)
    68,186
  • Last updated
    2010-11-30 v1
  • Checksum
    2E54368374F4F84F
MSNENRGPVPPRWLHCPRKAMRLIQGKFLAFKTPLSSAYDNQVPEECRFSVDMFFANLKSQKIKIGLWIDLTNTTRFYDRKTVEDYDCKYLKLQCRGHGETPSEEQTRTFVQVCRNFIAHNPLEIIGVHCTHGFNRTGFLIISYLLEIDGSSVDAALAEFATVRPPGIYKDDYIKELYRRYDDMDDAPPPPPRPSWCLECDDSNIEDVDEGPSTENENCHEEGQGKKRRREFNNKNPVFMAGVPGVTPILEKMRLSGIQKRVQEICGWKSTGFPGSQPVSMDVDNIMLLHTKPYRVSWKADGTRYMMLVQGDGEVYFIDRDNSVFEVNGLKFPHVRDINRCLRDTLMDGEMVIDKDKGKNIPRYLVYDVIMYDGQDVSKLMFHPDRYSIIESKIIAGRLKAMKEGRLVKEREPFSVRVKYFWDVTLSKDLLGEKFAKQLSHEPDGLIFQPAKEKYCAGVSPEVLKWKPQSLNSVDFRLKIVTETGVGILPRKVGHLYVGGLKTPYGVLPKLTKQLKELDNAIVECKFDNGQWIFMRQRVDKSFPNSRNTADSVYKSINKPVTKERLLEFIEKYRFIQDDSDLMPPPNKRPR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias213-233Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL435347
EMBL· GenBank· DDBJ
EFN73425.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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