Summary: Catalytic beta propeller domain of bacteriophage endosialidase
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Catalytic beta propeller domain of bacteriophage endosialidase Provide feedback
This domain family is found in bacteria and viruses, and is typically between 443 and 460 amino acids in length. This domain is the highly conserved beta propeller of bacteriophage endosialidase which represents the catalytically active part of the enzymes. This core domain forms stable SDS-resistant trimers. There is a nested beta barrel domain in this domain (PF12195). The endosialidase protein complexes to form a homotrimeric molecule.
Stummeyer K, Dickmanns A, Muhlenhoff M, Gerardy-Schahn R, Ficner R;, Nat Struct Mol Biol. 2005;12:90-96.: Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F. PUBMED:15608653 EPMC:15608653
Internal database links
|SCOOP:||BNR_2 BNR_3 Sortilin-Vps10 E1_FCCH|
|Similarity to PfamA using HHSearch:||End_beta_barrel|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024428This entry represents the beta propeller domain of endosialidases, which consists of catalytically active part of the enzymes. This core domain forms stable SDS-resistant trimers. There is a nested beta barrel domain in this domain. This domain is typically between 443 and 460 amino acids in length [PUBMED:15608653].
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This superfamily includes sialidases enzymes. Several viruses use sialic acid as a cell surface receptor for host invasion. These viruses then have cell surface neuraminidase enzymes to cleave sialic acid from cell surface proteins allowing them to leave the host cell after replication. This superfamily are composed of six beta-sheets that form a six-fold beta-propeller structure. Many members of this superfamily contain BNR sequence motifs Pfam:PF02012.
The clan contains the following 11 members:BNR BNR_2 BNR_3 BNR_4 BNR_6 End_beta_barrel End_beta_propel HN Neur PSII_BNR Sortilin-Vps10
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Author:||Mistry J, Gavin OL|
|Number in seed:||3|
|Number in full:||160|
|Average length of the domain:||415.60 aa|
|Average identity of full alignment:||88 %|
|Average coverage of the sequence by the domain:||46.05 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null --hand HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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There are 7 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 End_beta_propel domain has been found. There are 21 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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