DGQHR domain-containing protein showing similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system
DGQHR domain; This highly divergent, uncharacterized domain has several absolutely conserved ...
14-289
1.43e-70
DGQHR domain; This highly divergent, uncharacterized domain has several absolutely conserved residues, including a QR pair and FxxxN motif. Its most striking feature, however, is a near invariant pentapeptide motif DGQHR. Several different subfamilies occur specifically as a part of DNA phosphorothioation systems, previously called DND (DNA instability during electrophoresis), while others (e.g. CPS_2936) occur in other contexts suggestive of lateral gene transfer (sporadic distribution of helicase-containing cassettes). The region described by this model is about 280 amino acids in length; additional sequences show local sequence similarity.
:
Pssm-ID: 274476 Cd Length: 272 Bit Score: 224.07 E-value: 1.43e-70
DGQHR domain; This highly divergent, uncharacterized domain has several absolutely conserved ...
14-289
1.43e-70
DGQHR domain; This highly divergent, uncharacterized domain has several absolutely conserved residues, including a QR pair and FxxxN motif. Its most striking feature, however, is a near invariant pentapeptide motif DGQHR. Several different subfamilies occur specifically as a part of DNA phosphorothioation systems, previously called DND (DNA instability during electrophoresis), while others (e.g. CPS_2936) occur in other contexts suggestive of lateral gene transfer (sporadic distribution of helicase-containing cassettes). The region described by this model is about 280 amino acids in length; additional sequences show local sequence similarity.
Pssm-ID: 274476 Cd Length: 272 Bit Score: 224.07 E-value: 1.43e-70
DNA-sulfur modification-associated; This is family of bacterial proteins likely to be ...
12-293
1.20e-58
DNA-sulfur modification-associated; This is family of bacterial proteins likely to be necessary for binding to DNA and recognising the modification sites. Members are found in bacteria, archaea and on viral plasmids, and are typically between 354 and 474 amino acids in length. There is a conserved DGQHR sequence motif.
Pssm-ID: 433694 Cd Length: 337 Bit Score: 195.16 E-value: 1.20e-58
DNA sulfur modification protein DndB; dndB acts in the regulation of DNA modifications, ...
12-293
1.12e-53
DNA sulfur modification protein DndB; dndB acts in the regulation of DNA modifications, including DNA phosphorothioation. DndB may act by binding near the phosphorothioate modification site and regulating access of the Dnd modification machinery to DNA. These proteins show similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, and other members of the ParB/Srx superfamily.
Pssm-ID: 319269 Cd Length: 333 Bit Score: 182.14 E-value: 1.12e-53
DGQHR domain; This highly divergent, uncharacterized domain has several absolutely conserved ...
14-289
1.43e-70
DGQHR domain; This highly divergent, uncharacterized domain has several absolutely conserved residues, including a QR pair and FxxxN motif. Its most striking feature, however, is a near invariant pentapeptide motif DGQHR. Several different subfamilies occur specifically as a part of DNA phosphorothioation systems, previously called DND (DNA instability during electrophoresis), while others (e.g. CPS_2936) occur in other contexts suggestive of lateral gene transfer (sporadic distribution of helicase-containing cassettes). The region described by this model is about 280 amino acids in length; additional sequences show local sequence similarity.
Pssm-ID: 274476 Cd Length: 272 Bit Score: 224.07 E-value: 1.43e-70
DNA-sulfur modification-associated; This is family of bacterial proteins likely to be ...
12-293
1.20e-58
DNA-sulfur modification-associated; This is family of bacterial proteins likely to be necessary for binding to DNA and recognising the modification sites. Members are found in bacteria, archaea and on viral plasmids, and are typically between 354 and 474 amino acids in length. There is a conserved DGQHR sequence motif.
Pssm-ID: 433694 Cd Length: 337 Bit Score: 195.16 E-value: 1.20e-58
DNA sulfur modification protein DndB; dndB acts in the regulation of DNA modifications, ...
12-293
1.12e-53
DNA sulfur modification protein DndB; dndB acts in the regulation of DNA modifications, including DNA phosphorothioation. DndB may act by binding near the phosphorothioate modification site and regulating access of the Dnd modification machinery to DNA. These proteins show similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, and other members of the ParB/Srx superfamily.
Pssm-ID: 319269 Cd Length: 333 Bit Score: 182.14 E-value: 1.12e-53
DNA-sulfur modification-associated domain; Family of proteins related to dndB. dndB acts in ...
33-260
3.81e-51
DNA-sulfur modification-associated domain; Family of proteins related to dndB. dndB acts in the regulation of DNA modifications, including DNA phosphorothioation. Both have a conserved DGQHR sequence motif. These proteins show similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, and other members of the ParB/Srx superfamily
Pssm-ID: 319271 Cd Length: 238 Bit Score: 172.58 E-value: 3.81e-51
DGQHR motif containing domain; Uncharacterized diverse domain family with conserved DGQHR ...
51-164
2.58e-07
DGQHR motif containing domain; Uncharacterized diverse domain family with conserved DGQHR motif, in addition to QR and FXXXN motifs. Some proteins have been identified as parts of DNA phosphorothioation systems. Related to dndB, which acts in the regulation of DNA modifications, including DNA phosphorothioation. These proteins show similarity to the N-terminal domain of ParB, a DNA-binding component of the prokaryotic parABS partitioning system, and other members of the ParB/Srx superfamily.
Pssm-ID: 319270 Cd Length: 229 Bit Score: 51.19 E-value: 2.58e-07
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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