Protein Family Models

This entry represents an RNaseH-like domain found in the UvrC protein. Nucleotide excision repair (NER) is a conserved DNA repair pathway that enables the repair of chemically and structurally distinct DNA lesions. In prokaryotes, the UvrA, UvrB and UvrC proteins mediate NER in a multistep, ATP-dependent reaction. UvrC catalyses the first incision on the fourth or fifth phosphodiester bond 3' and on the eighth phosphodiester bond 5' from the damage that is to be excised. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain [2]. [1]. 8692686. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Doherty AJ, Serpell LC, Ponting CP;. Nucleic Acids Res 1996;24:2488-2497. [2]. 18439896. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Witte G, Hartung S, Buttner K, Hopfner KP;. Mol Cell. 2008;30:167-178. (from Pfam)

Date:

2024-10-16

This domain is found in the C subunits of the bacterial and archaeal UvrABC system which catalyses nucleotide excision repair in a multi-step process. UvrC catalyses the first incision on the fourth or fifth phosphodiester bond 3' and on the eighth phosphodiester bond 5' from the damage that is to be excised [1]. The domain described here represents the RNAse H endonuclease domain, located at the C-terminal, between the UvrBC and the (HhH)2 domains, nearby the N-terminal of the HhH. Despite the lack of sequence homology, the endonuclease domain has an RNase H-like fold, which is characteristic of enzymes with nuclease or polynucleotide transferase activities. RNase H-related enzymes typically contain a highly conserved carboxylate triad, usually DDE, in their catalytic centre. However, instead of a third carboxylate, UvrC of Thermotoga maritima was found to contain a highly conserved histidine (H488) on helix-4 in close proximity to two aspartates [1]. [1]. 17245438. Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad. Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C;. EMBO J. 2007;26:613-622. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

This domain called GIY-YIG is found in the amino terminal region of excinuclease abc subunit c (uvrC), bacteriophage T4 endonucleases segA, segB, segC, segD and segE; it is also found in putative endonucleases encoded by group I introns of fungi and phage. The structure of I-TevI a GIY-YIG endonuclease, reveals a novel alpha/beta-fold with a central three-stranded antiparallel beta-sheet flanked by three helices [4]. The most conserved and putative catalytic residues are located on a shallow, concave surface and include a metal coordination site. [1]. 1631169. Identification of a family of bacteriophage T4 genes encoding proteins similar to those present in group I introns of fungi and phage. Sharma M, Ellis RL, Hinton DM;. Proc Natl Acad Sci U S A 1992;89:6658-6662. [2]. 9973609. Conserved domains in DNA repair proteins and evolution of repair systems. Aravind L, Walker DR, Koonin EV;. Nucleic Acids Res 1999;27:1223-1242. [3]. 10219084. Configuration of the catalytic GIY-YIG domain of intron endonuclease I-TevI: coincidence of computational and molecular findings. Kowalski JC, Belfort M, Stapleton MA, Holpert M, Dansereau JT, Pietrokovski S, Baxter SM, Derbyshire V;. Nucleic Acids Res 1999;27:2115-2125. [4]. 12379841. Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI. Van Roey P, Meehan L, Kowalski JC, Belfort M, Derbyshire V;. Nat Struct Biol 2002;9:806-811. [5]. 16646971. Phylogenomic analysis of the GIY-YIG nuclease superfamily. Dunin-Horkawicz S, Feder M, Bujnicki JM;. BMC Genomics. 2006;7:98. (from Pfam)

Date:

2024-10-16

excinuclease ABC subunit UvrC is part of the UvrABC repair system that catalyzes the recognition and processing of DNA lesions

Date:

2024-10-09

Gene:

uvrC

Date:

2021-08-12