The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"DNA terminal protein Gp3, priming domain
".
The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"The DNA terminal protein Gp3 is linked to the 5' ends of both strands of the genome through a phosphodiester bond between the beta-hydroxyl group of a serine residue and the 5'-phosphate of the terminal deoxyadenylate. This protein is essential for DNA replication and is involved in the priming of DNA elongation PMID:6779279. In the transition from the initiation to the elongation phases, the priming domain of terminal protein moves out of the active site as polymerase elongates the primer strand. The terminal protein dissociates from the polymerase after the incorporation of approximately six nucleotides PMID:16511564.
This domain is a four-helix bundle with a left turning up-down-up-down topology. Serine-232, which provides the priming hydroxyl group for DNA synthesis, lies in a loop at the end of the domain closest to the active site of the DNA polymerase PMID:16511564.
DOI:10.1038/sj.emboj.7601027,PFAM:PF05435,INTERPRO:IPR008770
Structures | |
---|---|
Domains: | 6 |
Domain clusters (>95% seq id): | 1 |
Domain clusters (>35% seq id): | 1 |
Unique PDBs: | 1 |
Alignments | |
Structural Clusters (5A): | 1 |
Structural Clusters (9A): | 1 |
FunFam Clusters: | 1 |
Function | |
Unique EC: | |
Unique GO: | 3 |
Taxonomy | |
Unique Species: | 12 |