Summary: Insulinase (Peptidase family M16)
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Insulinase (Peptidase family M16) Provide feedback
No Pfam abstract.
Internal database links
SCOOP: | M16C_assoc Peptidase_M16_C |
External database links
HOMSTRAD: | Peptidase_M16 |
MEROPS: | M16 |
PROSITE: | PDOC00130 |
SCOP: | 1bgy |
This tab holds annotation information from the InterPro database.
InterPro entry IPR011765
This entry represents an N-terminal domain found in metallopeptidases and non-peptidase homologues belonging to MEROPS peptidase family M16 (clan ME), subfamilies M16A, M16B and M16C. Members of this family include:
- Insulinase, insulin-degrading enzyme (EC)
- Mitochondrial processing peptidase alpha subunit, (Alpha-MPP, EC)
- Pitrlysin, Protease III precursor (EC)
- Nardilysin, (EC)
- Ubiquinol-cytochrome C reductase complex core protein I,mitochondrial precursor (EC)
- Coenzyme PQQ synthesis protein F (EC)
These proteins do not share many regions of sequence similarity; the most noticeable is in the N-terminal section. This region includes a conserved histidine followed, two residues later by a glutamate and another histidine. In pitrilysin, it has been shown [PUBMED:7990931] that this H-x-x-E-H motif is involved in enzymatic activity; the two histidines bind zinc and the glutamate is necessary for catalytic activity. The proteins classified as non-peptidase homologues either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity.
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 Peptidase_ME (CL0094), which has the following description:
All members of this clan are characterised by a HXXEH motif, which is is involved in zinc binding. Furthermore all members adopt an alpha and beta fold. More specifically, there us a four to six stranded antiparallel beta sheet surrounded by five helices. However, LuxS (PFAM:PF02664) is not a peptidase, although its hydrolytic mechanism of catalysis appears to be conserved [1].
The clan contains the following 7 members:
LuxS M16C_assoc Peptidase_M16 Peptidase_M16_C Peptidase_M16_M Peptidase_M44 tRNA_SADAlignments
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...
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 (24) |
Full (27380) |
Representative proteomes | UniProt (65883) |
NCBI (94791) |
Meta (2153) |
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RP15 (7387) |
RP35 (17766) |
RP55 (26439) |
RP75 (35673) |
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HTML | |||||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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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 (24) |
Full (27380) |
Representative proteomes | UniProt (65883) |
NCBI (94791) |
Meta (2153) |
||||
---|---|---|---|---|---|---|---|---|---|
RP15 (7387) |
RP35 (17766) |
RP55 (26439) |
RP75 (35673) |
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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_88 (release 2.1) |
Previous IDs: | Insulinase; |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Bateman A |
Number in seed: | 24 |
Number in full: | 27380 |
Average length of the domain: | 136.10 aa |
Average identity of full alignment: | 21 % |
Average coverage of the sequence by the domain: | 22.47 % |
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: | 149 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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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Interactions
There are 14 interactions for this family. More...
UcrQ Peptidase_M16 Ubiq-Cytc-red_N UCR_14kD M16C_assoc Beta-APP Insulin Calc_CGRP_IAPP IL8 Hormone_2 UCR_14kD Peptidase_M16_C UCR_TM Peptidase_M16_CStructures
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_M16 domain has been found. There are 359 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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