Summary: Peptidase family M54
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Peptidase family M54 Provide feedback
This is a family of metallopeptidases. Two human proteins have been reported to degrade synthetic substrates and peptides .
Diaz-Perales A, Quesada V, Peinado JR, Ugalde AP, Alvarez J, Suarez MF, Gomis-Ruth FX, Lopez-Otin C; , J Biol Chem. 2005;280:30367-30375.: Identification and characterization of human archaemetzincin-1 and -2, two novel members of a family of metalloproteases widely distributed in Archaea. PUBMED:15972818 EPMC:15972818
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012962
This entry represents metzincins, which are zinc-dependent peptide-bond hydrolases. This family has a wide taxonomic distribution, being found in archaea, bacteria and eukaryotes. It was first identified in archaeal genomes and predicted to be zinc metalloproteases [PUBMED:20597090]. Two human homologues, archaemetzincin-1 and archaemetzincin-2, were also identified [PUBMED:15972818].
Interestingly, Human archaemetzincin-1 and archaemetzincin- 2 have aminopeptidase activity, while archaemetzincin from Mycococcus xanthus does not. Archaemetzincin (from Mycococcus xanthus) seem to have evolved into a zinc-binding transcription factor with the metal fulfilling only a structural role [PUBMED:15972818, PUBMED:20597090, PUBMED:16879646]. The structure of archaemetzincin from Methanopyrus kandleri has been resolved [PUBMED:20597090].
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|Molecular function||zinc ion binding (GO:0008270)|
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Clan MA is one of two zinc-dependent metallopeptidases that contain the HEXXH motif. The two histidines are zinc ligands. The structures of this clan show the active site is between its two sub-domains.
The clan contains the following 58 members:Aspzincin_M35 Astacin BSP DUF1570 DUF2201_N DUF2268 DUF3152 DUF3267 DUF3633 DUF3810 DUF4157 DUF4344 DUF45 DUF4953 DUF955 HRXXH Peptidase_M1 Peptidase_M10 Peptidase_M11 Peptidase_M13 Peptidase_M2 Peptidase_M27 Peptidase_M3 Peptidase_M30 Peptidase_M32 Peptidase_M35 Peptidase_M36 Peptidase_M4 Peptidase_M41 Peptidase_M43 Peptidase_M48 Peptidase_M4_C Peptidase_M50 Peptidase_M50B Peptidase_M54 Peptidase_M56 Peptidase_M57 Peptidase_M6 Peptidase_M60 Peptidase_M61 Peptidase_M64 Peptidase_M66 Peptidase_M7 Peptidase_M8 Peptidase_M9 Peptidase_M91 Peptidase_Mx Peptidase_Mx1 Peptidase_U49 Reprolysin Reprolysin_2 Reprolysin_3 Reprolysin_4 Reprolysin_5 SprT-like WLM Zn_peptidase Zn_peptidase_2
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_4509 (release 16.0)|
|Author:||Mistry J, Bateman A|
|Number in seed:||5|
|Number in full:||472|
|Average length of the domain:||127.60 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||53.66 %|
|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:||7|
|Download:||download the raw HMM for this family|
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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_M54 domain has been found. There are 7 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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