Protein Family Models

The bacterial protein RecR is an important regulator oin the RecFOR homologous recombination pathway during DNA repair. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a middle region containing a zinc finger motif (Pfam:PF02132) and a Toprim domain (Pfam:PF13662) and a C-terminal domain comprising a Walker B motif and a C-terminal helix (Pfam:PF21175) [1,2]. This is the HhH motif found at the N-temrinal of RecR which is essential for DNA binding and association with RecO [1,2]. [1]. 23019218. RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA. Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC;. Nucleic Acids Res. 2012;40:11115-11125. [2]. 29633970. Crystal structure of RecR, a member of the RecFOR DNA-repair pathway, from Pseudomonas aeruginosa PAO1. Che S, Chen Y, Liang Y, Zhang Q, Bartlam M;. Acta Crystallogr F Struct Biol Commun. 2018;74:222-230. (from Pfam)

Date:

2024-10-16

The bacterial protein RecR is an important regulator in the RecFOR homologous recombination pathway during DNA repair. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a middle region containing a zinc finger motif (Pfam:PF02132) and a Toprim domain (Pfam:PF13662), and a C-terminal domain comprising a Walker B motif and a C-terminal helix [1,2]. This is the C-terminal domain of RecR, which has a divergent Walker B motif, suggesting a nucleotide binding site [1,2]. [1]. 23019218. RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA. Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC;. Nucleic Acids Res. 2012;40:11115-11125. [2]. 29633970. Crystal structure of RecR, a member of the RecFOR DNA-repair pathway, from Pseudomonas aeruginosa PAO1. Che S, Chen Y, Liang Y, Zhang Q, Bartlam M;. Acta Crystallogr F Struct Biol Commun. 2018;74:222-230. (from Pfam)

Date:

2024-10-16

The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation [1]. [1]. 9722641. Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Aravind L, Leipe DD, Koonin EV;. Nucleic Acids Res 1998;26:4205-4213. (from Pfam)

Date:

2024-10-16

The bacterial protein RecR is an important regulator in the RecFOR homologous recombination pathway during DNA repair. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a middle region containing a zinc finger motif and a Toprim domain (Pfam:PF13662) and a C-terminal domain comprising a Walker B motif and a C-terminal helix [1,2]. This is the zinc finger motif, which consists of four strictly conserved cysteine residues which coordinate a zinc ion. This motif is the most conserved domain in RecR proteins and plays a structural role stabilizing the 3D structure of the protein [3]. [1]. 23019218. RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA. Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC;. Nucleic Acids Res. 2012;40:11115-11125. [2]. 29633970. Crystal structure of RecR, a member of the RecFOR DNA-repair pathway, from Pseudomonas aeruginosa PAO1. Che S, Chen Y, Liang Y, Zhang Q, Bartlam M;. Acta Crystallogr F Struct Biol Commun. 2018;74:222-230. [3]. 25460918. Structural and functional characterization of Cys4 zinc finger motif in the recombination mediator protein RecR. Tang Q, Liu YP, Yan XX, Liang DC;. DNA Repair (Amst). 2014;24:10-14. (from Pfam)

Date:

2024-10-16

This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins [1]. Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity [1]. DNA primase EC:2.7.7.6 is a nucleotidyltransferase it synthesises the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division [2]. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases [4]. Type II DNA topoisomerases catalyse the relaxation of DNA supercoiling by causing transient double strand breaks. [1]. 9722641. Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Aravind L, Leipe DD, Koonin EV;. Nucleic Acids Res 1998;26:4205-4213. [2]. 9224947. Cloning and analysis of the dnaG gene encoding Pseudomonas putida DNA primase. Szafranski P, Smith CL, Cantor CR;. Biochim Biophys Acta 1997;1352:243-248. [3]. 8294018. The Haemophilus influenzae dnaG sequence and conserved bacterial primase motifs. Versalovic J, Lupski JR;. Gene 1993;136:281-286. [4]. 9121560. An atypical topoisomerase II from Archaea with implications for meiotic recombination. Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P;. Nature 1997;386:414-417. (from Pfam)

Date:

2024-10-16

recombination protein RecR is a recombination mediator protein in the RecFOR pathway of homologous recombinational repair

Date:

2024-08-27

RecR mediates the initiation of recombination and recombinational repair. RecF is also required.

Gene:

recR

Date:

2024-05-30