Summary: X-Pro dipeptidyl-peptidase (S15 family)
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X-Pro dipeptidyl-peptidase (S15 family) Provide feedback
No Pfam abstract.
Internal database links
|Similarity to PfamA using HHSearch:||Abhydrolase_1 DLH Peptidase_S9 AXE1 Abhydrolase_3 BAAT_C Hydrolase_4 Abhydrolase_5 Abhydrolase_6|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000383
This entry represents a domain found peptidases Xaa-Pro dipeptidyl-peptidase and glutaryl-7-aminocephalosporanic-acid acylase, which belong to MEROPS peptidase families S15 and S45 respectively [PUBMED:7845208]. It is also found in hydrolases from the CocE/NonD family. Cocaine esterase (CocE) hydrolyzes cocaine endowing the bacteria with the ability to utilise cocaine as a sole source of carbon and energy [PUBMED:10698749].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||aminopeptidase activity (GO:0004177)|
|Biological process||proteolysis (GO:0006508)|
- 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
- the Pfam graphic itself.
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This catalytic domain is found in a very wide range of enzymes.
The clan contains the following 67 members:Abhydro_lipase Abhydrolase_1 Abhydrolase_2 Abhydrolase_3 Abhydrolase_4 Abhydrolase_5 Abhydrolase_6 Abhydrolase_7 Abhydrolase_8 Acyl_transf_2 Arb2 AXE1 BAAT_C Chlorophyllase Chlorophyllase2 COesterase Cutinase DLH DUF1057 DUF1100 DUF1350 DUF1400 DUF1749 DUF2048 DUF2235 DUF2305 DUF2424 DUF2920 DUF2974 DUF3089 DUF3141 DUF3530 DUF452 DUF676 DUF726 DUF818 DUF829 DUF900 DUF915 EHN Esterase Esterase_phd FSH1 Hydrolase_4 LCAT LIP Lipase Lipase_2 Lipase_3 Ndr PAF-AH_p_II Palm_thioest PE-PPE Peptidase_S10 Peptidase_S15 Peptidase_S28 Peptidase_S37 Peptidase_S9 PGAP1 PhaC_N PHB_depo_C PhoPQ_related Ser_hydrolase Tannase Thioesterase UPF0227 VirJ
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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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
|Seed source:||IPR000383 & Pfam-B_2704 (Release 7.5)|
|Author:||Mian N, Bateman A|
|Number in seed:||48|
|Number in full:||2545|
|Average length of the domain:||265.50 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||43.65 %|
|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:||13|
|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_S15 domain has been found. There are 54 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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