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exonuclease SbcCD subunit D C-terminal domain-containing protein
This domain is found in bacteria and archaea. This domain is about 90 amino acids in length. This domain is found associated with Pfam:PF00149. SbcD works in complex with SbdC (SbcDC) which is a transcription regulator. It down-regulates transcription of arl and mgr to inhibit type 5 capsule protein production. It acts as part of the SOS pathway of bacteria. [1]. 17704228. The sbcDC locus mediates repression of type 5 capsule production as part of the SOS response in Staphylococcus aureus. Chen Z, Luong TT, Lee CY;. J Bacteriol. 2007;189:7343-7350. (from Pfam)
metallophosphoesterase
This family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or yeast MRE11 Swiss:P32829. The most conserved regions in this superfamily centre around the metal chelating residues. [1]. 9685491. Phosphoesterase domains associated with DNA polymerases of diverse origins. Aravind L, Koonin EV;. Nucleic Acids Res 1998;26:3746-3752. (from Pfam)
exonuclease subunit SbcD
exonuclease SbcCD subunit D
exonuclease SbcCD subunit D is a component of SbcCD, which is involved in double-strand DNA break detection and repair by homologous recombination and non-homologous end joining of damaged DNA
All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
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