Summary: WASP-binding domain of Sorting nexin protein
WASP-binding domain of Sorting nexin protein Provide feedback
The C-terminal region of the Sorting nexin group of proteins appears to carry a BAR-like (Bin/amphiphysin/Rvs) domain. This domain is very diverse and the similarities with other BAR domains are few. In the Sorting nexins it is associated with family PX, PF00787.13, and in combination with PX appears to be necessary to bind WASP along with p85 to form a multimeric signalling complex .
Yarar D, Waterman-Storer CM, Schmid SL; , Dev Cell. 2007;13:43-56.: SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. PUBMED:17609109 EPMC:17609109
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR019497
The C-terminal region of the Sorting nexin group of proteins appears to carry a BAR-like (Bin/amphiphysin/Rvs) domain. This domain is very diverse and the similarities with other BAR domains are few. In the Sorting nexins it is associated with INTERPRO, and in combination with PX appears to be necessary to bind WASP along with p85 to form a multimeric signalling complex [PUBMED:14993925].
- the number of sequences which exhibit this architecture
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
- the UniProt description of the protein sequence
- the number of residues in the sequence
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This clan contains families that are involved in intracellular transport and signalling. Arfaptins are proteins which interact with small GTPases involved in vesicular budding at the Golgi complex. They form an elongated dimer of three helix coiled coils and are structurally very similar to the BAR domain . The Sec34 family is involved in tethering vesicles to the Golgi .
The clan contains the following 8 members:Arfaptin BAR BAR_2 BAR_3 BAR_3_WASP_bdg FAM92 IMD Vps5
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
You can see the alignments as HTML or in three different sequence viewers:
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Curation and family details
|Seed source:||Pfam-B_43522 (release 20.0)|
|Number in seed:||7|
|Number in full:||2336|
|Average length of the domain:||124.40 aa|
|Average identity of full alignment:||73 %|
|Average coverage of the sequence by the domain:||43.22 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -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 BAR_3_WASP_bdg domain has been found. There are 10 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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