Summary: Signal peptidase, peptidase S26
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Signal peptidase, peptidase S26 Provide feedback
This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesised secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR019533
This entry represents a domain found in some members of the S26A/S25C family of serine endopeptidases. Peptidases S26A (signal peptidase I) removes the hydrophobic, N-terminal signal peptides as proteins are translocated across membranes. Peptidases 26C (TraF signal peptidase) are found in operons that encode elements of conjugative transfer systems.
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EGFdomains, and finally a single
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This clan includes the peptidase S24 and S26 families. These families adopt a mainly beta fold. Members of the family S24 have an additional C-terminal domain containing a bundle of three helices presumably important for binding DNA.
The clan contains the following 3 members:Peptidase_S24 Peptidase_S26 Phage_CI_C
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 UniProtKB sequence database using the family HMM
- 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
|Author:||Mistry J. Rawlings N|
|Number in seed:||25|
|Number in full:||1291|
|Average length of the domain:||98.10 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||37.83 %|
|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:||6|
|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 Peptidase_S26 domain has been found. There are 17 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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