Summary: Baseplate structural protein, domain 2
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Baseplate structural protein, domain 2 Provide feedback
Members of this family adopt a beta barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. They are structural component of the viral baseplate, predominantly found in the structural protein gp27 .
Kanamaru S, Leiman PG, Kostyuchenko VA, Chipman PR, Mesyanzhinov VV, Arisaka F, Rossmann MG; , Nature 2002;415:553-557.: Structure of the cell-puncturing device of bacteriophage T4. PUBMED:11823865 EPMC:11823865
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015180
This domain adopts a beta barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. It is found at the C terminus of the Gp27 protein; a structural component of the viral baseplate [PUBMED:11823865].
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a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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This superfamily consists of a variety of bacteriophage protein families. Structurally members of this family contain a beta barrel.
The clan contains the following 8 members:DUF2001 Gifsy-2 Minor_tail_Z Phage-tail_1 Phage-tail_2 Phage-tail_3 Phage_attach Phage_GPD
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Number in seed:||6|
|Number in full:||29|
|Average length of the domain:||166.00 aa|
|Average identity of full alignment:||58 %|
|Average coverage of the sequence by the domain:||42.44 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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There are 2 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 Phage-tail_2 domain has been found. There are 3 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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