Retroviral aspartyl protease
| Retroviral aspartyl protease | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | RVP | ||||||||
| Pfam | PF00077 | ||||||||
| InterPro | IPR001995 | ||||||||
| PROSITE | PDOC00128 | ||||||||
| SCOP | 1ida | ||||||||
| SUPERFAMILY | 1ida | ||||||||
| OPM superfamily | 108 | ||||||||
| OPM protein | 2b7z | ||||||||
| |||||||||
Retroviral aspartyl proteases are single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger pol or gag polyprotein. Retroviral proteases are homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (Pfam PF00026).
Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised.[1] More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin[2] and archaean preflagellin have been described.[3][4]
Structurally, aspartic endopeptidases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe has probably evolved from the other through a gene duplication event in the distant past. In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent, except for the catalytic site motif, which is very conserved. The presence and position of disulphide bridges are other conserved features of aspartic peptidases. All or most aspartate peptidases are endopeptidases. These enzymes have been assigned into clans (proteins which are evolutionary related), and further sub-divided into families, largely on the basis of their tertiary structure.
Retroviral aspartyl protease is synthesised as part of the POL polyprotein that contains; an aspartyl protease, a reverse transcriptase, RNase H and integrase. POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins.
Human proteins containing this domain
References
- ↑ Szecsi PB (1992). "The aspartic proteases". Scand. J. Clin. Lab. Invest. Suppl. 210: 5–22. doi:10.3109/00365519209104650. PMID 1455179.
- ↑ Taylor RK, LaPointe CF (2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". J. Biol. Chem. 275 (2): 1502–10. doi:10.1074/jbc.275.2.1502. PMID 10625704.
- ↑ Jarrell KF, Ng SY, Chaban B (2006). "Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications". J. Mol. Microbiol. Biotechnol. 11 (3): –. doi:10.1159/000094053. PMID 16983194.
- ↑ Jarrell KF, Bardy SL (2003). "Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae". Mol. Microbiol. 50 (4): 1339–1347. doi:10.1046/j.1365-2958.2003.03758.x. PMID 14622420.
This article incorporates text from the public domain Pfam and InterPro IPR001995