Protein Family Models

Date:

2024-08-14

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:

2024-08-14

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:

2024-08-14

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:

2024-08-14

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

Date:

2022-07-25

Gene:

uvrC

Date:

2021-08-12

The UvrABC repair system catalyzes the recognition and processing of helix-distorting DNA lesions, such as those caused by UV light, for Nucleotide Excision Repair (NER). UvrC cuts on both the 5' and the 3' side of the lesion.

Gene:

uvrC

Date:

2021-04-27