Summary: mRNA capping enzyme, beta chain
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mRNA capping enzyme, beta chain Provide feedback
The beta chain of mRNA capping enzyme has triphosphatase activity. The function of the capping enzyme also depends on the guanylyltransferase activity conferred by the alpha chain (see PF01331)
Yamada-Okabe T, Mio T, Matsui M, Kashima Y, Arisawa M, Yamada-Okabe H; , FEBS Lett 1998;435:49-54.: Isolation and characterization of the Candida albicans gene for mRNA 5'-triphosphatase: association of mRNA 5'-triphosphatase and mRNA 5'-guanylyltransferase activities is essential for the function of mRNA 5'-capping enzyme in vivo. PUBMED:9755857 EPMC:9755857
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004206
The mRNA capping enzyme in yeast is composed of two subunits, alpha and beta. The alpha subunit has guanylyltransferase activity, whilst the beta subunit is an RNA 5'-triphosphatase [PUBMED:9345280].
This entry represents a structural domain found in the mRNA capping enzyme beta subunit. The domain is related to the CYTH domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||polynucleotide 5'-phosphatase activity (GO:0004651)|
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CyaB like adenylyl cyclase and the mammalian thiamine triphosphatases define a novel superfamily of catalytic domains called the CYTH domain that is present in all three superkingdoms of life. The catalytic core of these enzymes contain a novel alpha beta scaffold with 6 conserved acidic residues and 4 basic residues .
The clan contains the following 2 members:CYTH mRNA_triPase
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Curation and family details
|Seed source:||Structural domain|
|Number in seed:||18|
|Number in full:||274|
|Average length of the domain:||217.00 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||41.64 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the mRNA_triPase domain has been found. There are 16 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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