Argos P, Landy A, Abremski K, Egan J B, Haggard-Ljungquist E, Hoess R H, Kahn M L, Kalionis B, Narayana S V, Pierson L S
EMBO J. 1986 Feb;5(2):433-40. doi: 10.1002/j.1460-2075.1986.tb04229.x.
A combination of two methods for detecting distant relationships in protein primary sequences was used to compare the site-specific recombination proteins encoded by bacteriophage lambda, phi 80, P22, P2, 186, P4 and P1. This group of proteins exhibits an unexpectedly large diversity of sequences. Despite this diversity, all of the recombinases can be aligned in their C-terminal halves. A 40-residue region near the C terminus is particularly well conserved in all the proteins and is homologous to a region near the C terminus of the yeast 2 mu plasmid Flp protein. This family of recombinases does not appear to be related to any other site-specific recombinases. Three positions are perfectly conserved within this family: histidine, arginine and tyrosine are found at respective alignment positions 396, 399 and 433 within the well-conserved C-terminal region. We speculate that these residues contribute to the active site of this family of recombinases, and suggest that tyrosine-433 forms a transient covalent linkage to DNA during strand cleavage and rejoining.
运用两种检测蛋白质一级序列中远距离关系的方法，对噬菌体λ、φ80、P22、P2、186、P4和P1所编码的位点特异性重组蛋白进行了比较。这组蛋白呈现出意想不到的序列多样性。尽管存在这种多样性，但所有的重组酶在其C端半段都可以比对。C端附近一个40个残基的区域在所有蛋白质中都特别保守，并且与酵母2μm质粒Flp蛋白C端附近的一个区域同源。这个重组酶家族似乎与任何其他位点特异性重组酶都没有关系。在这个家族中有三个位置完全保守：在保守的C端区域内，分别在比对位置396、399和433处发现组氨酸、精氨酸和酪氨酸。我们推测这些残基对这个重组酶家族的活性位点有贡献，并表明酪氨酸-433在链切割和重新连接过程中与DNA形成瞬时共价连接。
