EC Number   |
Subunits |
Reference |
|---|
   2.7.7.B16 | ? |
x * 29000, Rep245 domain containing the N-terminal domain of the pIT3 replication protein encompassing residues 31245, SDS-PAGE |
-, 719447 |
| 2.7.7.B16 | ? |
x * 41800, calculated from sequence |
-, 720567 |
| 2.7.7.B16 | heterodimer |
- |
-, 719444, 720015, 720228, 720489 |
| 2.7.7.B16 | heterodimer |
1 * 36000 + 1 * 38000, SDS-PAGE |
-, 720572 |
| 2.7.7.B16 | heterodimer |
1 * 41000 + 1 * 46000, calculated from sequence |
720231 |
| 2.7.7.B16 | heterodimer |
1 * 46209 (large subunit Pfup46) + 1 * 40772 (small subunit Pfup41), calculated from sequence |
719808 |
| 2.7.7.B16 | heterotrimer |
archaea encode a eukaryotic-type primase comprising a catalytic subunit, PriS, and a noncatalytic subunit, PriL and PriX. PriX is a diverged homologue of the C-terminal domain of PriL but lacks the iron-sulfur cluster. PriX, PriL and PriS form a stable heterotrimer (PriSLX). Both PriSX and PriSLX show far greater affinity for nucleotide substrates and are substantially more active in primer synthesis than the PriSL heterodimer. PriL, but not PriX, facilitates primer extension by PriS. The catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis. PriX subunit residues 26-54 are in a flexible region. PriX residues 55-154 fold into a single domain containing 6 helices, which form a compact core stabilized by extensive hydrophobic interactions. The overall structure of the PriX protein is quite unique, sequence and three-dimensional structure comparisons, overview |
739147 |
| 2.7.7.B16 | More |
the Pfup46 protein increases the affinity of the primase to DNA by forming a complex with the catalytic Pfup41 subunit |
719808 |
