Proteins containing this domain include Escherichia coli plasmid protein ParB and mammalian Sulfiredoxin-1. ParB is involved in chromosome partition. It localize to both poles of the predivisional cell following completion of DNA replication []. Sulfiredoxin-1 contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4 [].
Proteins containing this domain include Escherichia coli plasmid protein ParB and mammalian Sulfiredoxin-1. ParB is involved in chromosome partition. It localize to both poles of the predivisional cell following completion of DNA replication []. Sulfiredoxin-1 contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4 [].The structure of ParB/Sulfiredoxin has a beta-α-β(2)-α-β-alpha fold with mixed beta sheet forming a partly open barrel.
This entry represents the catalytic domain of the Serine/Threonine Kinase, RPK118 (also known as ribosomal protein S6 kinase delta-1) and similar proteins. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. This domain is also present in human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains a MIT domain, but lacks a PX domain.RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling []. RPK118 also binds the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria [].
