Summary: Carboxypeptidase activation peptide
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Carboxypeptidase activation peptide Provide feedback
Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase, and is responsible for modulation of folding and activity of the pro-enzyme.
Literature references
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Aloy P, Catasus L, Villegas V, Reverter D, Vendrell J, Aviles FX; , Biol Chem 1998;379:149-155.: Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B. PUBMED:9524066 EPMC:9524066
External database links
MEROPS: | M14 |
PROSITE: | PDOC00123 |
SCOP: | 1pba |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003146
The peptidases are synthesised as inactive molecules, zymogens, with propeptides that must be removed by proteolytic cleavage to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended alpha-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by making specific contacts [PUBMED:7674922, PUBMED:1548696].
This entry represents a propeptide associated with peptidases belonging to MEROPS peptidase family M14A. It is found in the carboxypeptidases A [PUBMED:9384570] and B [PUBMED:12162965].
Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (propeptide or activation peptide) accounts for up to a quarter of the total length of the peptidase.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | carboxypeptidase activity (GO:0004180) |
Biological process | proteolysis (GO:0006508) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan PPP-I (CL0570), which has the following description:
This superfamily is characterised by families of short N-terminal domains such as the pancreatic carboxypeptidase activation domain, the subtilase propeptides/inhibitors, the prohormone convertase 1 pro-domain, and the peptidase- S8 pro-domain. All families exbhibit an alpha+beta sandwich with antiparallel beta-sheets in a (beta-alpha-beta)x2 conformation.
The clan contains the following 6 members:
Inhibitor_I9 Pro-kuma_activ Pro_sub2 Propep_M14 S8_pro-domain Tk-SP_N-proAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (388) |
Full (2520) |
Representative proteomes | UniProt (4433) |
NCBI (5092) |
Meta (2) |
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RP15 (630) |
RP35 (1143) |
RP55 (1970) |
RP75 (2374) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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Seed (388) |
Full (2520) |
Representative proteomes | UniProt (4433) |
NCBI (5092) |
Meta (2) |
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RP15 (630) |
RP35 (1143) |
RP55 (1970) |
RP75 (2374) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_2335 (release 5.2) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 388 |
Number in full: | 2520 |
Average length of the domain: | 72.00 aa |
Average identity of full alignment: | 22 % |
Average coverage of the sequence by the domain: | 15.75 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 73 | ||||||||||||
Family (HMM) version: | 16 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
Structures
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 Propep_M14 domain has been found. There are 33 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 sequence.
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