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DNA-processing protein DprA, partial [Brochothrix sp.]
LOG family protein( domain architecture ID 366823)
LOG (Lonely Guy) family protein may function as a hydrolase, similar to Arabidopsis thaliana cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG1 that converts inactive cytokinin nucleotides to the biologically active free-base forms
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
Smf super family | cl34034 | Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake ... |
15-168 | 4.30e-67 | |||
Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake [Replication, recombination and repair]; The actual alignment was detected with superfamily member COG0758: Pssm-ID: 440521 [Multi-domain] Cd Length: 360 Bit Score: 208.01 E-value: 4.30e-67
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Name | Accession | Description | Interval | E-value | ||||
Smf | COG0758 | Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake ... |
15-168 | 4.30e-67 | ||||
Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake [Replication, recombination and repair]; Pssm-ID: 440521 [Multi-domain] Cd Length: 360 Bit Score: 208.01 E-value: 4.30e-67
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DNA_processg_A | pfam02481 | DNA recombination-mediator protein A; The SMF family, of DNA processing chain A, dprA, are a ... |
1-160 | 1.28e-60 | ||||
DNA recombination-mediator protein A; The SMF family, of DNA processing chain A, dprA, are a group of bacterial proteins. In H. pylori, dprA is required for natural chromosomal and plasmid transformation. It has now been shown that DprA is found to bind cooperatively to single-stranded DNA (ssDNA) and to interact with RecA. In the process, DprA-RecA-ssDNA filaments are produced and these filaments catalyze the homology-dependent formation of joint molecules. While the E.coli SSB protein limits access of RecA to ssDNA, DprA alleviates this barrier. It is proposed that DprA is a new member of the recombination-mediator protein family, dedicated to natural bacterial transformation. Pssm-ID: 426793 Cd Length: 210 Bit Score: 186.59 E-value: 1.28e-60
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dprA | TIGR00732 | DNA protecting protein DprA; Disruption of this gene in both Haemophilus influenzae and ... |
2-167 | 1.97e-51 | ||||
DNA protecting protein DprA; Disruption of this gene in both Haemophilus influenzae and Helicobacter pylori drastically reduces the efficiency of transformation with exogenous DNA, but with different levels of effect on chromosomal (linear) and plasmid (circular) DNA. This difference suggests the DprA is not active in recombination, and it has been shown not to affect DNA binding, leaving the intermediate step in natural transformation, DNA processing. In Strep. pneumoniae, inactivation of dprA had no effect on the uptake of DNA. All of these data indicated that DprA is required at a later stage in transformation. Subsequently DprA and RecA were both shown in S. pneumoniae to be required to protect incoming ssDNA from immediate degradation. Role of DprA in non-transformable species is not known. The gene symbol smf was assigned in E. coli, but without assignment of function. [Cellular processes, DNA transformation] Pssm-ID: 273238 Cd Length: 220 Bit Score: 163.65 E-value: 1.97e-51
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PRK10736 | PRK10736 | DNA-protecting protein DprA; |
18-168 | 3.18e-38 | ||||
DNA-protecting protein DprA; Pssm-ID: 236747 [Multi-domain] Cd Length: 374 Bit Score: 133.92 E-value: 3.18e-38
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Name | Accession | Description | Interval | E-value | ||||
Smf | COG0758 | Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake ... |
15-168 | 4.30e-67 | ||||
Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake [Replication, recombination and repair]; Pssm-ID: 440521 [Multi-domain] Cd Length: 360 Bit Score: 208.01 E-value: 4.30e-67
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DNA_processg_A | pfam02481 | DNA recombination-mediator protein A; The SMF family, of DNA processing chain A, dprA, are a ... |
1-160 | 1.28e-60 | ||||
DNA recombination-mediator protein A; The SMF family, of DNA processing chain A, dprA, are a group of bacterial proteins. In H. pylori, dprA is required for natural chromosomal and plasmid transformation. It has now been shown that DprA is found to bind cooperatively to single-stranded DNA (ssDNA) and to interact with RecA. In the process, DprA-RecA-ssDNA filaments are produced and these filaments catalyze the homology-dependent formation of joint molecules. While the E.coli SSB protein limits access of RecA to ssDNA, DprA alleviates this barrier. It is proposed that DprA is a new member of the recombination-mediator protein family, dedicated to natural bacterial transformation. Pssm-ID: 426793 Cd Length: 210 Bit Score: 186.59 E-value: 1.28e-60
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dprA | TIGR00732 | DNA protecting protein DprA; Disruption of this gene in both Haemophilus influenzae and ... |
2-167 | 1.97e-51 | ||||
DNA protecting protein DprA; Disruption of this gene in both Haemophilus influenzae and Helicobacter pylori drastically reduces the efficiency of transformation with exogenous DNA, but with different levels of effect on chromosomal (linear) and plasmid (circular) DNA. This difference suggests the DprA is not active in recombination, and it has been shown not to affect DNA binding, leaving the intermediate step in natural transformation, DNA processing. In Strep. pneumoniae, inactivation of dprA had no effect on the uptake of DNA. All of these data indicated that DprA is required at a later stage in transformation. Subsequently DprA and RecA were both shown in S. pneumoniae to be required to protect incoming ssDNA from immediate degradation. Role of DprA in non-transformable species is not known. The gene symbol smf was assigned in E. coli, but without assignment of function. [Cellular processes, DNA transformation] Pssm-ID: 273238 Cd Length: 220 Bit Score: 163.65 E-value: 1.97e-51
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PRK10736 | PRK10736 | DNA-protecting protein DprA; |
18-168 | 3.18e-38 | ||||
DNA-protecting protein DprA; Pssm-ID: 236747 [Multi-domain] Cd Length: 374 Bit Score: 133.92 E-value: 3.18e-38
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Blast search parameters | ||||
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