Protein Family Models

This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homologue SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains [1,2,3,4]. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region [4]. [1]. 26896444. Structural mechanism of ATP-dependent DNA binding and DNA end. bridging by eukaryotic Rad50.. Seifert FU, Lammens K, Stoehr G, Kessler B, Hopfner KP;. EMBO J. 2016;35:759-772.. [2]. 21892167. The Rad50 coiled-coil domain is indispensable for Mre11 complex. functions.. Hohl M, Kwon Y, Galvan SM, Xue X, Tous C, Aguilera A, Sung P,. Petrini JH;. Nat Struct Mol Biol. 2011;18:1124-1131.. [3]. 28134932. Eukaryotic Rad50 functions as a rod-shaped dimer.. Park YB, Hohl M, Padjasek M, Jeong E, Jin KS, Krezel A, Petrini. JH, Cho Y;. Nat Struct Mol Biol. 2017;24:248-257.. [4]. 31492634. Mechanism of DNA End Sensing and Processing by the Mre11-Rad50. Complex.. Kashammer L, Saathoff JH, Lammens K, Gut F, Bartho J, Alt A,. Kessler B, Hopfner KP;. Mol Cell. 2019;76:382-394. (from Pfam)

Date:

2024-04-03

This domain is found in a number of double-strand DNA break proteins. This domain contains a P-loop motif. (from Pfam)

Date:

2023-12-12

Date:

2023-12-12

AAA family ATPase with an AAA (ATPases Associated with various cellular Activities) domain catalyzes the hydrolysis of ATP to form ADP and phosphate, and couples the energy released by the reaction to drive fundamental biological processes; ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATPase; AAA family ATPase with an AAA (ATPases Associated with various cellular Activities) domain catalyzes the hydrolysis of ATP to form ADP and phosphate, and couples the energy released by the reaction to drive fundamental biological processes; ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATPase; ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as the toxin for a type IV toxin-antitoxin resistance system; AAA family ATPase with an AAA (ATPases Associated with various cellular Activities) domain catalyzes the hydrolysis of ATP to form ADP and phosphate, and couples the energy released by the reaction to drive fundamental biological processes; ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATPase; ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain, may function as the toxin for a type IV toxin-antitoxin resistance system; ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATPase; ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, similar to putative AbiEii toxin, the type IV toxin-antitoxin (TA) system that has a toxin and an antitoxin, which interferes with the binding of the toxin to its target; OLD (overcoming lysogenization defect)-family ATP-dependent endonuclease may have DNAse as well as RNAse activity; recF family protein; ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATPase

Date:

2017-09-25