Summary: Proprotein convertase P-domain
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Proprotein convertase P-domain Provide feedback
A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.
Gluschankof P, Fuller RS; , EMBO J 1994;13:2280-2288.: A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease. PUBMED:8194519 EPMC:8194519
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This tab holds annotation information from the InterPro database.
InterPro entry IPR002884
This domain, termed the P domain is approximately 150 amino acids in length and C-terminal to a serine endopeptidase domain which belong to MEROPS peptidase family S8 (clan SB), subfamily S8B (kexin). The domain is primarily associated with the calcium-dependent serine endopeptidases, kex2/subtilisin proprotein convertases (PCs), which have been identified in all eukaryotes [PUBMED:9353231] and in the gammaproteobacteria, Nostoc (cyanobacteria) and in Streptomyces avermitilis.
The P domain appears necessary for folding and maintaining the endopeptidase catalytic domain and to regulate its calcium and acidic pH dependence. In addition, contained within the middle of the P domain in most PC family members is the cognate integrin binding RGD sequence [PUBMED:10212221], which may be required for intracellular compartmentalization and maintenance of enzyme stability within the ER. The integrity of the RGD sequence of proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking [PUBMED:9307023, PUBMED:10212221]. The carboxy-terminal tail provides uniqueness to each PC family member being the least conserved region of all convertases [PUBMED:10842308].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||serine-type endopeptidase activity (GO:0004252)|
|Biological process||proteolysis (GO:0006508)|
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This large superfamily contains beta sandwich domains with a jelly roll topology. Many of these families are involved in carbohydrate recognition. Despite sharing little sequence similarity they do share a weak sequence motif, with a conserved bulge in the C-terminal beta sheet. The probable role of this bulge is in bending of the beta sheet that contains the bulge. This enables the curvature of the sheet forming the sugar binding site .
The clan contains the following 32 members:Allantoicase ANAPC10 Bac_rhamnosid_N BetaGal_dom4_5 CBM-like CBM27 CBM60 CBM_11 CBM_15 CBM_17_28 CBM_35 CBM_4_9 CBM_6 CIA30 DUF5000 DUF642 Endotoxin_C Ephrin_lbd F5_F8_type_C FBA Glyco_hydro_2_N Laminin_N Lyase_N Muskelin_N NPCBM P_proprotein PA-IL PepX_C PITH PPC Sad1_UNC XRCC1_N
We make a range of alignments for each Pfam-A family:
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
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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:||45|
|Number in full:||2904|
|Average length of the domain:||87.60 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||11.40 %|
|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:||16|
|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 P_proprotein domain has been found. There are 27 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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