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Links from Protein

Items: 11

1.

RecR, helix-hairpin-helix

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
Family Accession:
NF045310.2
Method:
HMM
2.

RecR, C-terminal

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
Family Accession:
NF044419.2
Method:
HMM
3.

toprim domain-containing protein

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
Family Accession:
NF025044.5
Method:
HMM
4.

RecR, Cys4-zinc finger motif

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)

GO Terms:
Molecular Function:
metal ion binding (GO:0046872)
Date:
2024-10-16
Family Accession:
NF014217.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

recombination mediator RecR

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

Date:
2024-08-27
Family Accession:
11417471
Method:
Sparcle
11.

recombination mediator RecR

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

Gene:
recR
GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Biological Process:
DNA repair (GO:0006281)
Biological Process:
DNA recombination (GO:0006310)
Molecular Function:
metal ion binding (GO:0046872)
Date:
2024-05-30
Family Accession:
TIGR00615.1
Method:
HMM
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