The following text describes a protein:
Function:
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by mre11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, rad50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (By similarity). Rad50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the mre11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the atm and atr kinases: the nuclease activity of mre11 is not required to activate ATM and ATR (By similarity). The MRN complex promotes recruitment of topbp1 to DNA damage sites. The MRN complex and rbbp8/CtIP are also required for chromosome alignment during metaphase.
Subcellular Localization:
Nucleus. Chromosome, telomere. Chromosome. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs).
Domain:
The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer.
Sequence:
MSKIEKMSIQGVRSFGINDKNKQVIQFFTPLTILVGPNGAGKTTIIECLKYMTTGDFPSGSKGNTFVYHPKLAHETDVRAQICLQLKDVNGEPVAVQRSIICRQKGKSTECKTVDCVITRIKHGGPVSLRPKCEEMNKEMISALGVSSAVLNNVIFCHQEDSNWPLSEGKRLKGKFDEIFSITRYSKALETLRDVRMKEDQNVSNYQEEIKYLKENKEKAREIQDNLQSKEKQLTVSKENVKSIESQLEPLKDRLADIQRNLFKVIRLENEIKALESRKRTMEQDNQDLMEKMEKVFQGTDEELNEMYQNQCFVREKERKLNDHQREMDRACKESQRLNREKGELLVQQGHLQLEADNHQRYIKTRDSLIKSLAVQLELDGFELTPFNQRQTSNFQMLVKERQEEVEAHANQILREFSEREAMQQRQIDEIRDKKTGLERTIELKSSTESKKHTDLKKVKYDLQQLEGTSDRLHELDEELQKTAHALENVEKSCNLEALKGEVVQLQTQKSELDRNVRELDQEMEQLNKHTMTRTQMDMLKNDKADKDEQIRKMKSRHNDELISLYEYFPNKKQLEDWLYSKREDINQTRDKLARLTKELVAAEQNSNHLSNELCQKEKQSASFEEKVFDVCGSQDFNSDLSQLLEDIEKTSKQRAMLAGATAVYTQFITTLTEENQPCCPVCQRTFPSEAEVQDVINDMQSKLCLVPDKLKAAEDELKRKEKRKDEMMELKPMRQMLSDLKEKEIPEIRNKLEAINREIKRLQNDVEEQESLIVTFVSEEARAEACLQDISLMEQYQMELRDVDQKIAHYATKLLGVDLNRTVQQVNQEKLEKHHSLDNVSRRIELLQNHLQNQQEQVQQLKSRVNELTAEKLHISSNLQQRQQLEEQNVELTTELHCLSIEIKESREQVFPLESTLQKLQQEKQALLQRKESSYREAQEKVNDIKEKVKKINLHTKDIEKYIQDGKEEFKEQKESELQELTVRLNECEELKEKINREMVTIRQDIDTQKIQERCLQDNLTLRKRIEELKQVEEERDQLLKEMGQMKVTQMEKEYQELENKRETLKTNHSLTLGRQKGFEDEILRFKNELNEPKYKDAEEEYREKMIVMRTTELAIKDLDIYFKTMDQAIMKFHSIKMEEINKIIRDLWCSTYRGQDIEYIEIQSEPDEGISAADNRRTYNYRVVMIKGDTELDMRGHCSAGQKVLASLIIRLALAEIFCSNCGVLALDEPTTNLDHENIDSLAHALVEIIKSRSRQRNFQLIVITHNEDFVELLGRSEYVEHFYRIKKNIDQCSEIIRCSVSSLASYLH