| Primary Identifier | IPR020084 | Type | Conserved_site |
| Short Name | NUDIX_hydrolase_CS |
| description | MutT is a small bacterial protein (~12-15Kd) involved in the GO system []responsible for removing an oxidatively damaged form of guanine (8-hydroxy-guanine or 7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool.8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with near equal efficiency, leading to A.T to G.C transversions. MutTspecifically degrades 8-oxo-dGTP to the monophosphate, with the concomitantrelease of pyrophosphate. A short conserved N-terminal region of mutT (designated the MutT domain) is also found in a variety of otherprokaryotic, viral and eukaryotic proteins [, , , ].The generic name `NUDIX hydrolases' (NUcleoside DIphosphate linkedto some other moiety X) has been coined for this domain family []. Thefamily can be divided into a number of subgroups, of which MutT anti-mutagenic activity represents only one type; most of the rest hydrolysediverse nucleoside diphosphate derivatives (including ADP-ribose, GDP-mannose, TDP-glucose, NADH, UDP-sugars, dNTP and NTP).This signature covers the core region of the NUDIX domain and contains four conserved glutamate residues []. The region spanned by this signature could be part of the active centre of a family of pyrophosphate-releasing NTPases. |
