| Retroviral aspartyl protease | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 HIV-1 proteasedimer in white and grey, with peptidesubstrate in black andactive site aspartate side chains in red. (PDB:1KJF) | |||||||||
| Identifiers | |||||||||
| Symbol | RVP | ||||||||
| Pfam | PF00077 | ||||||||
| InterPro | IPR001995 | ||||||||
| PROSITE | PDOC00128 | ||||||||
| MEROPS | A2 | ||||||||
| SCOP2 | 1ida /SCOPe /SUPFAM | ||||||||
| OPM superfamily | 100 | ||||||||
| OPM protein | 2q63 | ||||||||
| Membranome | 532 | ||||||||
| |||||||||
Retroviral aspartyl proteases orretropepsins are single domainaspartyl proteases fromretroviruses,retrotransposons, andbadnaviruses (plantdsDNA viruses). These proteases are generally part of a largerpol orgagpolyprotein. Retroviral proteases are homologous to a single domain of the two-domain eukaryoticaspartyl proteases such aspepsins,cathepsins, andrenins (PfamPF00026;MEROPS A1). Retropepsins are members of MEROPS A2, clan AA. All known members areendopeptidases.
The enzyme is only active as ahomodimer, as each one corresponds to half of the eukaryotic two-lobe enzyme. The two parts each contribute one catalytic aspartyl residue.[1]
Retroviral aspartyl protease is synthesised as part of the pol polyprotein that contains anaspartyl protease, areverse transcriptase,RNase H andintegrase. pol polyprotein undergoes specific enzymatic cleavage to yield the mature proteins.
Not all retroviral aspartyl proteases generated frompol are retropepsins in the strict sense. Spumapepsin fromfoamy virus is divergent enough to get its own family, MEROPS A9. Many other examples are found in clan AA.
