This is the VRR-NUC domain, a member of the PD-(D/E)XK nuclease superfamily found in FAN1 and type III restriction modification enzymes [1]. FAN1 is a a structure-selective DNA repair nuclease with 5' flap endonuclease activity, involved in the repair of interstrand DNA crosslinks [2,3]. FAN1 is the only eukaryotic protein with a VRR-NUC domain. This domain is also found in TseVs antibacterial effectors secreted by the type VI secretion system (T6SS). TseVs are evolutionary related to Holliday junction resolvases and enzymes involved in DNA interstrand crosslink repair [4]. [1]. 15972856. Identification of novel restriction endonuclease-like fold families among hypothetical proteins. Kinch LN, Ginalski K, Rychlewski L, Grishin NV;. Nucleic Acids Res. 2005;33:3598-3605. [2]. 24981866. FAN1 activity on asymmetric repair intermediates is mediated by an atypical monomeric virus-type replication-repair nuclease domain. Pennell S, Declais AC, Li J, Haire LF, Berg W, Saldanha JW, Taylor IA, Rouse J, Lilley DM, Smerdon SJ;. Cell Rep. 2014;8:84-93. [3]. 29514982. Structural mechanism of DNA interstrand cross-link unhooking by the bacterial FAN1 nuclease. Jin H, Roy U, Lee G, Scharer OD, Cho Y;. J Biol Chem. 2018;293:6482-6496. [4]. 36226828. Antibacterial T6SS effectors with a VRR-Nuc domain are structure-specific nucleases. Hespanhol JT, Sanchez-Limache DE, Nicastro GG, Mead L, Llontop EE, Chagas-Santos G, Farah CS, de Souza RF, Galhardo RDS, Lovering AL, Bayer-Santos E;. Elife. 2022;11:e82437. (from Pfam)
GO Terms:- Molecular Function:
- hydrolase activity, acting on ester bonds (GO:0016788)
- Date:
- 2024-10-16