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0  structures 232  species 0  interactions 4408  sequences 86  architectures

Family: Neprosin (PF03080)

Summary: Neprosin

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Neprosin Provide feedback

Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. The neprosin domain corresponds to the mature peptidase [1]. It is not known if other proteins with this domain are peptidases.

Literature references

  1. Rey M, Yang M, Lee L, Zhang Y, Sheff JG, Sensen CW, Mrazek H, Halada P, Man P, McCarville JL, Verdu EF, Schriemer DC;, Sci Rep. 2016;6:30980.: Addressing proteolytic efficiency in enzymatic degradation therapy for celiac disease. PUBMED:27481162 EPMC:27481162


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004314

Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. The neprosin domain corresponds to the mature peptidase [ PUBMED:27481162 ]. It is not known if other proteins with this domain are peptidases.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

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 and the UniProtKB sequence database. More...

View options

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
(160)
Full
(4408)
Representative proteomes UniProt
(6432)
RP15
(427)
RP35
(2067)
RP55
(3521)
RP75
(4845)
Jalview View  View  View  View  View  View  View 
HTML View  View           
PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(160)
Full
(4408)
Representative proteomes UniProt
(6432)
RP15
(427)
RP35
(2067)
RP55
(3521)
RP75
(4845)
Alignment:
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Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(160)
Full
(4408)
Representative proteomes UniProt
(6432)
RP15
(427)
RP35
(2067)
RP55
(3521)
RP75
(4845)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

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 View help on the curation process

Seed source: Pfam-B_913 (release 6.4)
Previous IDs: DUF239; Glucoamylase; DUF239;
Type: Family
Sequence Ontology: SO:0100021
Author: Griffiths-Jones SR
Number in seed: 160
Number in full: 4408
Average length of the domain: 180.50 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 53.72 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.0 21.5
Trusted cut-off 22.0 21.5
Noise cut-off 21.9 21.4
Model length: 213
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0N7KEH6 View 3D Structure Click here
A0A0N7KMK5 View 3D Structure Click here
A0A0N7KSD8 View 3D Structure Click here
A0A0N7KU31 View 3D Structure Click here
A0A0P0V2L2 View 3D Structure Click here
A0A0P0V3U9 View 3D Structure Click here
A0A0P0V3Z1 View 3D Structure Click here
A0A0P0VA29 View 3D Structure Click here
A0A0P0VQL0 View 3D Structure Click here
A0A0P0VQL5 View 3D Structure Click here
A0A0P0VQN5 View 3D Structure Click here
A0A0P0WIV0 View 3D Structure Click here
A0A0P0WL17 View 3D Structure Click here
A0A0P0WSZ2 View 3D Structure Click here
A0A0P0WVJ8 View 3D Structure Click here
A0A0P0X2S9 View 3D Structure Click here
A0A0P0X579 View 3D Structure Click here
A0A0P0XFW6 View 3D Structure Click here
A0A0P0Y005 View 3D Structure Click here
A0A0P0Y0I5 View 3D Structure Click here
A0A0P0Y0R3 View 3D Structure Click here
A0A0P0Y151 View 3D Structure Click here
A0A0P0Y1G2 View 3D Structure Click here
A0A0P0YAM2 View 3D Structure Click here
A0A0R0EF07 View 3D Structure Click here
A0A0R0FHB8 View 3D Structure Click here
A0A0R0GJV0 View 3D Structure Click here
A0A0R0GN02 View 3D Structure Click here
A0A0R0HUJ1 View 3D Structure Click here
A0A0R0IVM9 View 3D Structure Click here
A0A0R0JC82 View 3D Structure Click here
A0A0R0K2G1 View 3D Structure Click here
A0A0R4J2M5 View 3D Structure Click here
A0A1D6FEU3 View 3D Structure Click here
A0A1D6HVP7 View 3D Structure Click here
A0A1D6J4N2 View 3D Structure Click here
A0A1D6KLR3 View 3D Structure Click here
A0A1D6L8F9 View 3D Structure Click here
A0A1D6LUT0 View 3D Structure Click here
A0A1D6LUT2 View 3D Structure Click here
A0A1D6LZP1 View 3D Structure Click here
A0A1D6MKC0 View 3D Structure Click here
A0A1D6MTW9 View 3D Structure Click here
A0A1D6MY28 View 3D Structure Click here
A0A1D6MY28 View 3D Structure Click here
A0A1D6NMX7 View 3D Structure Click here
A0A1D6P0D0 View 3D Structure Click here
A0A1P8B3Z8 View 3D Structure Click here
A0A1P8B6J1 View 3D Structure Click here
A0A1P8B762 View 3D Structure Click here
A0A1P8B762 View 3D Structure Click here
A0A1P8BDW2 View 3D Structure Click here
B4G0L1 View 3D Structure Click here
B9DGK6 View 3D Structure Click here
C6T970 View 3D Structure Click here
F4I5H4 View 3D Structure Click here
F4ISH3 View 3D Structure Click here
F4ISW5 View 3D Structure Click here
F4IT63 View 3D Structure Click here
F4IT66 View 3D Structure Click here
F4IU76 View 3D Structure Click here
F4JJC7 View 3D Structure Click here
F4JLL3 View 3D Structure Click here
F4JLL4 View 3D Structure Click here
F4JMS0 View 3D Structure Click here
F4JNI5 View 3D Structure Click here
F4JNI6 View 3D Structure Click here
F4JNI7 View 3D Structure Click here
F4JNI8 View 3D Structure Click here
F4JP70 View 3D Structure Click here
F4JWS2 View 3D Structure Click here
F4JYA0 View 3D Structure Click here
F4JYA1 View 3D Structure Click here
F4JYY1 View 3D Structure Click here
F4JZN1 View 3D Structure Click here
F4K4G7 View 3D Structure Click here
F4K779 View 3D Structure Click here
I1J562 View 3D Structure Click here
I1JRU1 View 3D Structure Click here
I1K029 View 3D Structure Click here
I1KSP0 View 3D Structure Click here
I1MTE8 View 3D Structure Click here
I1N1K0 View 3D Structure Click here
I1NCE9 View 3D Structure Click here
I1NIL2 View 3D Structure Click here
K7KKZ0 View 3D Structure Click here
K7KVQ6 View 3D Structure Click here
K7KZW4 View 3D Structure Click here
K7L9H1 View 3D Structure Click here
K7LEQ7 View 3D Structure Click here
K7M6Q5 View 3D Structure Click here
K7M8E3 View 3D Structure Click here
K7M8E4 View 3D Structure Click here
K7U8I5 View 3D Structure Click here
O64859 View 3D Structure Click here
O82168 View 3D Structure Click here
Q0J3L1 View 3D Structure Click here
Q1PE74 View 3D Structure Click here
Q1PE81 View 3D Structure Click here
Q1PF53 View 3D Structure Click here
Q5BPS8 View 3D Structure Click here
Q5JK80 View 3D Structure Click here
Q5VQM6 View 3D Structure Click here
Q653W6 View 3D Structure Click here
Q69Y39 View 3D Structure Click here
Q6ZIY2 View 3D Structure Click here
Q6ZL19 View 3D Structure Click here
Q84JS7 View 3D Structure Click here
Q84JV5 View 3D Structure Click here
Q84M37 View 3D Structure Click here
Q8GX31 View 3D Structure Click here
Q8GXV8 View 3D Structure Click here
Q8GY67 View 3D Structure Click here
Q8LFH3 View 3D Structure Click here
Q8VYE1 View 3D Structure Click here
Q941C9 View 3D Structure Click here
Q9C8A7 View 3D Structure Click here
Q9FF71 View 3D Structure Click here
Q9FG96 View 3D Structure Click here
Q9FGP1 View 3D Structure Click here
Q9FIP3 View 3D Structure Click here
Q9FIP4 View 3D Structure Click here
Q9LJE0 View 3D Structure Click here
Q9LVC1 View 3D Structure Click here
Q9LYG4 View 3D Structure Click here
Q9SK38 View 3D Structure Click here
Q9SL64 View 3D Structure Click here

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;