A0A0C7N7F2 · A0A0C7N7F2_9SACH

  • Protein
    mRNA-capping enzyme subunit alpha
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.

Catalytic activity

Features

Showing features for active site.

147150100150200250300350400450
TypeIDPosition(s)Description
Active site66N6-GMP-lysine intermediate

GO annotations

AspectTerm
Cellular ComponentmRNA capping enzyme complex
Molecular FunctionATP binding
Molecular FunctionGTP binding
Molecular FunctionmRNA guanylyltransferase activity
Biological Process7-methylguanosine mRNA capping

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    mRNA-capping enzyme subunit alpha
  • EC number
  • Alternative names
    • GTP--RNA guanylyltransferase
    • mRNA guanylyltransferase

Gene names

    • ORF names
      LALA0_S05e06304g

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 12615
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Lachancea

Accessions

  • Primary accession
    A0A0C7N7F2

Proteomes

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Heterodimer. The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain43-245mRNA capping enzyme adenylation
Domain249-393mRNA capping enzyme C-terminal
Compositional bias404-424Basic and acidic residues
Region404-471Disordered
Compositional bias425-439Polar residues
Compositional bias443-460Acidic residues

Sequence similarities

Belongs to the eukaryotic GTase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    471
  • Mass (Da)
    54,276
  • Last updated
    2015-04-29 v1
  • Checksum
    41E4FE1FEB0A9021
MDSRVSPEIPGIRLPASVMQDIRMLVCKLLNSPKPTKTFPGSQPISFHHSDIEEKLLAQDYYVCEKTDGLRGLMLMVINPVTKEQGCFIIDRENNYFQVSGFRFPRLPKQSRKELLETFQDGTLIDGELVIQTNPVTKLKELRYLMFDCLAINGRCIAQSPTSSRLAHLGKEFFKPYYDLRSLYPAQCSTFPFKISMKVMNFSTDLSKVAHSLDKLPHVSDGLIFTPVNTPYTIGGKDSLLLKWKPEEENSVDFKMILEIPLAEDTSLPKNDANRFYHNYEVKPSFHLYTWQGGADVNARLQAFDQPFSKKELDLLDRTYKKFAELEISNEKWQELKSLDEPLNGRVVECTKDQETGVWHMLRFRDDKLNGNHVSVVKKVLESISDSVKIEDLEEATTKMKENWQLRHSDRKRSFQEAHRPSASEDVDLNTTNGGQSFKQPDYVDDDDEDDDDMWPDNDEDLETEPKKPKL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias404-424Basic and acidic residues
Compositional bias425-439Polar residues
Compositional bias443-460Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LN736364
EMBL· GenBank· DDBJ
CEP62467.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp