Family A9
Summary for family A9
Name | Peptidase family A9 (spumapepsin family) |
Family type peptidase | A09.001 - spumapepsin (human spumaretrovirus), MEROPS Accession MER0001439 (peptidase unit: 14-180) |
Content of family | Peptidase family A9 contains an endopeptidase, spumapepsin. |
History |
Identifier created: Proteolysis in Cell Function, pp13-21, IOS Press, Amsterdam (1997)
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Catalytic type | Aspartic |
Active site residues | D24 |
Active site | The active site Asp of spumapepsin has been identified by site-directed mutagenesis (Konvalinka et al., 1995), and like other viral endopeptidases in clan AA, spumapepsin is assumed to be active only as a dimer with one Asp from each monomer forming the active site dyad. The active site Asp occurs in a Asp-Xaa-Gly motif where Xaa is Ser or Thr. No sequence equivalent to the pepsin (A01.001) 'flap' has been identified. |
Activities and specificities | Spumapepsin processes both the Gag and Pol viral polyproteins. Four cleavages are made, all except one being at asparaginyl bonds. Spumapepsin has also been shown to cleave Pol polyproteins of the yeast Ty1 and Ty3 retrotransposons (Fenyofalvi et al., 1999). Cleavage occurs at neutral pH. |
Inhibitors | No inhibitors have been reported. |
Molecular structure | The tertiary structure of spumapepsin has not been determined. In human foamy virus, spumapepsin is part of the Gag polyprotein, but in simian foamy virus it is part of the Pol polyprotein (Renne et al., 1992). The presence of the motif Asp-Ser/Thr-Gly around the active site Asp in both spumapepsin and pepsin, the type example of clan AA, is the basis for the inclusion of family A9 in clan AA. |
Clan | AA |
Basis of clan assignment | Active site residues for members of this family and family A1 occur in the motif D-T/S-G. |
Distribution of family
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Bacteria |
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Archaea |
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Protozoa |
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Fungi |
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Plants |
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Animals |
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Viruses |
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Peptidases and Homologues |
MEROPS ID |
Structure |
spumapepsin | A09.001 | Yes |
Family A09 unassigned peptidases | unassigned | - |