exodeoxyribonuclease VII large subunit is a component of bacterial exonuclease VII which degrades ssDNA and is involved in DNA repair and recombination
exodeoxyribonuclease VII, large subunit; This family consist of exodeoxyribonuclease VII, ...
6-439
9.09e-168
exodeoxyribonuclease VII, large subunit; This family consist of exodeoxyribonuclease VII, large subunit XseA which catalyses exonucleolytic cleavage in either the 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. Exonuclease VII consists of one large subunit and four small subunits. [DNA metabolism, Degradation of DNA]
Pssm-ID: 272979 [Multi-domain] Cd Length: 389 Bit Score: 476.54 E-value: 9.09e-168
Exonuclease VII, large subunit; This family consist of exonuclease VII, large subunit EC:3.1. ...
123-437
1.01e-105
Exonuclease VII, large subunit; This family consist of exonuclease VII, large subunit EC:3.1.11.6 This enzyme catalyzes exonucleolytic cleavage in either 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. This exonuclease VII enzyme is composed of one large subunit and 4 small ones.
Pssm-ID: 426865 Cd Length: 264 Bit Score: 313.99 E-value: 1.01e-105
ExoVII_LU_OBF: A subfamily of OB folds corresponding to the N-terminal OB-fold domain of ...
26-102
8.87e-31
ExoVII_LU_OBF: A subfamily of OB folds corresponding to the N-terminal OB-fold domain of Escherichia coli exodeoxyribonuclease VII (ExoVII) large subunit. E. coli ExoVII is composed of two non-identical subunits. E. coli ExoVII is a single-strand-specific exonuclease which degrades ssDNA from both 3-prime and 5-prime ends. ExoVII plays a role in methyl-directed mismatch repair in vivo. ExoVII may also guard the genome from mutagenesis by removing excess ssDNA, since the build up of ssDNA would lead to SOS induction and PolIV-dependent mutagenesis.
Pssm-ID: 239935 [Multi-domain] Cd Length: 78 Bit Score: 113.38 E-value: 8.87e-31
exodeoxyribonuclease VII, large subunit; This family consist of exodeoxyribonuclease VII, ...
6-439
9.09e-168
exodeoxyribonuclease VII, large subunit; This family consist of exodeoxyribonuclease VII, large subunit XseA which catalyses exonucleolytic cleavage in either the 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. Exonuclease VII consists of one large subunit and four small subunits. [DNA metabolism, Degradation of DNA]
Pssm-ID: 272979 [Multi-domain] Cd Length: 389 Bit Score: 476.54 E-value: 9.09e-168
Exonuclease VII, large subunit; This family consist of exonuclease VII, large subunit EC:3.1. ...
123-437
1.01e-105
Exonuclease VII, large subunit; This family consist of exonuclease VII, large subunit EC:3.1.11.6 This enzyme catalyzes exonucleolytic cleavage in either 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. This exonuclease VII enzyme is composed of one large subunit and 4 small ones.
Pssm-ID: 426865 Cd Length: 264 Bit Score: 313.99 E-value: 1.01e-105
ExoVII_LU_OBF: A subfamily of OB folds corresponding to the N-terminal OB-fold domain of ...
26-102
8.87e-31
ExoVII_LU_OBF: A subfamily of OB folds corresponding to the N-terminal OB-fold domain of Escherichia coli exodeoxyribonuclease VII (ExoVII) large subunit. E. coli ExoVII is composed of two non-identical subunits. E. coli ExoVII is a single-strand-specific exonuclease which degrades ssDNA from both 3-prime and 5-prime ends. ExoVII plays a role in methyl-directed mismatch repair in vivo. ExoVII may also guard the genome from mutagenesis by removing excess ssDNA, since the build up of ssDNA would lead to SOS induction and PolIV-dependent mutagenesis.
Pssm-ID: 239935 [Multi-domain] Cd Length: 78 Bit Score: 113.38 E-value: 8.87e-31
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
27-100
5.17e-11
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 58.40 E-value: 5.17e-11
RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold ...
29-100
2.50e-03
RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold of the single strand (ss) DNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). RPA contains six OB folds, which are involved in ssDNA binding and in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. This family also includes OB folds similar to those found in Escherichia coli SSB, the wedge domain of E. coli RecG (a branched-DNA-specific helicase), E. coli ssDNA specific exodeoxyribonuclease VII large subunit, Pyrococcus abyssi DNA polymerase II (Pol II) small subunit, Sulfolobus solfataricus SSB, and Bacillus subtilis YhaM (a 3'-to-5'exoribonuclease). It also includes the OB folds of breast cancer susceptibility gene 2 protein (BRCA2), Oxytricha nova telomere end binding protein (TEBP), Saccharomyces cerevisiae telomere-binding protein (Cdc13), and human protection of telomeres 1 protein (POT1).
Pssm-ID: 239601 [Multi-domain] Cd Length: 75 Bit Score: 36.57 E-value: 2.50e-03
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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