ID 3.4.22.66 DE calicivirin. AN calicivirus 3C-like protease. AN calicivirus endopeptidase. AN calicivirus TCP. AN calicivirus trypsin-like cysteine protease. AN Camberwell virus processing peptidase. AN Chiba virus processing peptidase. AN norovirus virus processing peptidase. AN Norwalk virus processing peptidase. AN rabbit hemorrhagic disease virus 3C endopeptidase. AN Southampton virus processing peptidase. CA Endopeptidase with a preference for cleavage when the P1 position is CA occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa. CC -!- Viruses that are members of the Norovirus genus (Caliciviridae CC family) are a major cause of epidemic acute viral gastroenteritis. CC -!- The non-structural proteins of these viruses are produced by CC proteolytic cleavage of a large precursor polyprotein, performed by a CC protease that is incorporated into the polyprotein. CC -!- Cleavage sites are apparently defined by features based on both CC sequence and structure since several sites in the polyprotein CC fulfilling the identified sequence requirements are not cleaved. CC -!- The presence of acidic (Asp), basic (Arg), aromatic (Tyr) or CC aliphatic (Leu) amino acids at the P1' position results in only minor CC differences in cleavage efficiency, suggesting that steric or CC conformational constraints may play a role in determining CC specificity. CC -!- Changes to the amino acid at the P2 position do not alter cleavage CC efficiency. CC -!- Belongs to peptidase family C37. DR Q288N7, POLG_BECN1 ; Q8JN60, POLG_BECNB ; Q8V736, POLG_CACV4 ; DR Q96725, POLG_EBHSG ; N0A3C0, POLG_FCV ; P27407, POLG_FCVC6 ; DR P27408, POLG_FCVF4 ; P27409, POLG_FCVF9 ; Q66914, POLG_FCVUR ; DR P54634, POLG_LORDV ; Q83883, POLG_NVN68 ; Q9QEJ5, POLG_PESV ; DR P27411, POLG_RHDV3 ; Q86119, POLG_RHDVA ; Q89273, POLG_RHDVB ; DR P27410, POLG_RHDVF ; Q86117, POLG_RHDVS ; P36286, POLG_SMSV1 ; DR P36287, POLG_SMSV4 ; Q04544, POLG_SOUV3 ; Q6XDK8, POLG_SVM10 ; DR Q69014, POLG_SVM93 ; Q672I1, POLG_SVSAP ; Q9DUN3, POLG_VESVA ; //