Summary: Peptidase M16 inactive domain
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Peptidase M16 inactive domain Provide feedback
Peptidase M16 consists of two structurally related domains. One is the active peptidase, whereas the other is inactive. The two domains hold the substrate like a clamp .
Taylor AB, Smith BS, Kitada S, Kojima K, Miyaura H, Otwinowski Z, Ito A, Deisenhofer J; , Structure (Camb) 2001;9:615-625.: Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. PUBMED:11470436 EPMC:11470436
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007863
These metallopeptidases belong to MEROPS peptidase family M16 (clan ME). They include proteins, which are 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.
The peptidases in this group of sequences 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 mitochondrial processing peptidase consists of two structurally related domains. One is the active peptidase whereas the other, the C-terminal region, is inactive. The two domains hold the substrate like a clamp [PUBMED:11470436].
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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 .
The clan contains the following 4 members:LuxS Peptidase_M16 Peptidase_M16_C Peptidase_M44
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Yeats C|
|Number in seed:||139|
|Number in full:||56090|
|Average length of the domain:||179.30 aa|
|Average identity of full alignment:||16 %|
|Average coverage of the sequence by the domain:||37.42 %|
|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:||17|
|Download:||download the raw HMM for this family|
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There are 20 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_M16_C domain has been found. There are 307 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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