v5.1.0.3
Glycine data from LIS
Type | Homologous_superfamily |
Description | This entry represents a β-barrel domain consisting of a duplication of a beta/alpha/beta/alpha/beta motif, which is found in plant cyclic phosphodiesterases (CPDases) [ ], as well as catalytic domains from mammalian 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) [], and bacterial and archaeal LigT-like 2',3'-cyclic phosphodiesterases (originally identified as 2'-5' RNA ligases) []. This β-barrel domain is similar in structure to the β-barrel found in prokaryotic DNA topoisomerases I and III.The catalytic domain of CNPase from animals catalyzes the hydrolysis of nucleoside 2',3'-cyclic monophosphates to nucleoside 2'-monophosphates [ ]. The archaeobacterial LigT-like enzymes hydrolyze 2',3'-cyclic phosphate in (oligo)nucleotides and join the produced 2'-phosphate to a 5'-hydroxyl group of another (oligo)nucleotide to form atypical 2',5'-linkages. Such activity has not been reported for CNPase []. |
Short Name | Cyclic_Pdiesterase |