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Protein Domain : IPR006026

Name  Peptidase, metallopeptidase Short Name  Peptidase_Metallo
Type  Domain Description  In the MEROPS database peptidases and peptidase homologues are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry based on a common structural fold:Each clan is identified with two letters, the first representing the catalytic type of the families included in the clan (with the letter 'P' being used for a clan containing families of more than one of the catalytic types serine, threonine and cysteine). Some families cannot yet be assigned to clans, and when a formal assignment is required, such a family is described as belonging to clan A-, C-, M-, N-, S-, T- or U-, according to the catalytic type. Some clans are divided into subclans because there is evidence of a very ancient divergence within the clan, for example MA(E), the gluzincins, and MA(M), the metzincins.Peptidase families are grouped by their catalytic type, the first character representing the catalytic type: A, aspartic; C, cysteine; G, glutamic acid; M, metallo; N, asparagine; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine peptidases utilise the amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated water molecule. In the case of the asparagine endopeptidases, the nucleophile is asparagine and all are self-processing endopeptidases. In many instances the structural protein fold that characterises the clan or family may have lost its catalytic activity, yet retain its function in protein recognition and binding. Metalloproteases are the most diverse of the four main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site []. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [].The majority of zinc-dependent metallopeptidases (with the notable exceptionof the carboxypeptidases) share a common pattern of primary structure [, ]in the part of their sequence involved in the binding of zinc, and can begrouped together as a superfamily,known as the metzincins, on the basis ofthis sequence similarity. They can be classified into around 40 distinct families []. This signature defines the metallopeptidases associated with MEROPS peptidase families: M7, M8, M10 (subfamilies A, B and C) and M12 (subfamily A) all of which are members of clan MA(M).
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Publication Counts Displayer

2 Child Features

DB identifier Name Short Name Type
IPR001506 Peptidase M12A, astacin Peptidase_M12A Domain
IPR001818 Peptidase M10, metallopeptidase Pept_M10_metallopeptidase Domain

0 Contains

1 Cross References

Identifier
Source . Name
Subject . Primary Identifier
SM00235 SMART IPR006026

3 Data Sets

Name URL
Swiss-Prot data set http://ca.expasy.org/sprot
InterPro data set  
InterPro GO Annotation data set  

12 Found In

DB identifier Name Short Name Type
IPR017050 Peptidase M12A, astacin, nematode Peptidase_M12A_nem Family
IPR017367 Peptidase M12A, nematode astacin 7/8 Peptidase_M12A_astacin-7/8 Family
IPR021190 Peptidase M10A Pept_M10A Family
IPR016293 Peptidase M10A, stromelysin-type Pept_M10A_stromelysin-type Family
IPR017368 Peptidase M12A, nematode astacin 9/10/11 Peptidase_M12A_astacin-9/10/11 Family
IPR015446 Bone morphogenetic protein 1/tolloid-like protein BMP_1/tolloid-like Family
IPR016294 Peptidase M10B Pept_M10B Family
IPR017369 SPAN protein/blastula protease 10 SPAN/blastula_protease_10 Family
IPR017370 Hatching enzyme, Uvs2 Hatching_enzyme_Uvs2 Family
IPR008294 Meprin alpha/beta subunit Meprin Family
IPR001843 Peptidase M10C, fragilysin Pept_M10C Family
IPR022603 Domain of unknown function DUF3152 DUF3152 Domain

3 GO Annotation


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Peptidase, metallopeptidase   GO:0008237 metallopeptidase activity
Peptidase, metallopeptidase   GO:0008270 zinc ion binding
Peptidase, metallopeptidase   GO:0006508 proteolysis

3 Ontology Annotations


Subject . Secondary Identifier
Subject . Name
Subject . Symbol
Ontology Term . Identifier
Ontology Term . Name
Peptidase, metallopeptidase   GO:0008237 metallopeptidase activity
Peptidase, metallopeptidase   GO:0008270 zinc ion binding
Peptidase, metallopeptidase   GO:0006508 proteolysis

0 Parent Features

340 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0078297 Q9VNK5 Drosophila melanogaster
FBpp0080342 Q9VJN9 Drosophila melanogaster
FBpp0082501 Q9VFD6 Drosophila melanogaster
FBpp0074382 Q9VWR6 Drosophila melanogaster
FBpp0083770 Q9VCN5 Drosophila melanogaster
FBpp0084069 Q9VC47 Drosophila melanogaster
FBpp0080340 Q9V421 Drosophila melanogaster
FBpp0084018 Q9VC98 Drosophila melanogaster
FBpp0080343 Q9V445 Drosophila melanogaster
FBpp0080312 Q9V402 Drosophila melanogaster
FBpp0087585 Q8MPP3 Drosophila melanogaster
FBpp0080313 Q9V3R0 Drosophila melanogaster
FBpp0080341 Q9V3M3 Drosophila melanogaster
FBpp0084070 P25723 Drosophila melanogaster
FBpp0271771 Q9W122 Drosophila melanogaster
FBpp0271772 Q8MLN6 Drosophila melanogaster
FBpp0307322 B5E0D1 Drosophila pseudoobscura
FBpp0287786 Q29KV7 Drosophila pseudoobscura
FBpp0272266 Q29FZ0 Drosophila pseudoobscura
FBpp0306119 N6W524 Drosophila pseudoobscura
FBpp0278520 Q28XL6 Drosophila pseudoobscura
FBpp0281582 Q296J1 Drosophila pseudoobscura
FBpp0282336 Q29A67 Drosophila pseudoobscura
FBpp0282875 Q29BZ7 Drosophila pseudoobscura
FBpp0282876 B5DXS7 Drosophila pseudoobscura
FBpp0284091 Q297X5 Drosophila pseudoobscura
FBpp0284249 Q297B8 Drosophila pseudoobscura
FBpp0287528 Q29KV9 Drosophila pseudoobscura
FBpp0287527 Q29KV8 Drosophila pseudoobscura
FBpp0287529 B5DJL4 Drosophila pseudoobscura




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