Nucleic acid-binding proteins superfamily [Arabidopsis thaliana]
replication protein A OB-fold DNA-binding domain-containing protein; single-stranded DNA-binding protein( domain architecture ID 10138918)
replication protein A (RPA) OB-fold DNA-binding domain-containing protein| single-stranded DNA (ssDNA)-binding protein plays a key role in DNA replication, recombination, and repair
List of domain hits
Name | Accession | Description | Interval | E-value | |||
RPA1_DBD_C | cd04476 | RPA1_DBD_C: A subfamily of OB folds corresponding to the C-terminal OB fold, the ssDNA-binding ... |
110-252 | 1.73e-25 | |||
RPA1_DBD_C: A subfamily of OB folds corresponding to the C-terminal OB fold, the ssDNA-binding domain (DBD)-C, of human RPA1 (also called RPA70). RPA1 is the large 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). In addition to DBD-C, RPA1 contains three other OB folds: DBD-A, DBD-B, and RPA1N. The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in DNA binding and trimerization. It contains two structural insertions not found to date in other OB-folds: a zinc ribbon and a three-helix bundle. RPA1 DBD-C also contains a Cys4-type zinc-binding motif, which plays a role in the ssDNA binding function of this domain. It appears that zinc itself may not be required for ssDNA binding. : Pssm-ID: 239922 [Multi-domain] Cd Length: 166 Bit Score: 99.69 E-value: 1.73e-25
|
|||||||
RPA1_DBD_A_like | cd04480 | RPA1_DBD_A_like: A subgroup of uncharacterized plant OB folds with similarity to the second OB ... |
23-80 | 3.03e-13 | |||
RPA1_DBD_A_like: A subgroup of uncharacterized plant OB folds with similarity to the second OB fold, the ssDNA-binding domain (DBD)-A, of human RPA1 (also called RPA70). RPA1 is the large 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). In addition to DBD-A, RPA1 contains three other OB folds: DBD-B, DBD-C, and RPA1N. The major DNA binding activity of RPA is associated with DBD-A and DBD-B of RPA1. RPA1 DBD-C is involved in trimerization. The ssDNA-binding mechanism is believed to be multistep and to involve conformational change. : Pssm-ID: 239926 [Multi-domain] Cd Length: 86 Bit Score: 64.20 E-value: 3.03e-13
|
|||||||
Name | Accession | Description | Interval | E-value | |||
RPA1_DBD_C | cd04476 | RPA1_DBD_C: A subfamily of OB folds corresponding to the C-terminal OB fold, the ssDNA-binding ... |
110-252 | 1.73e-25 | |||
RPA1_DBD_C: A subfamily of OB folds corresponding to the C-terminal OB fold, the ssDNA-binding domain (DBD)-C, of human RPA1 (also called RPA70). RPA1 is the large 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). In addition to DBD-C, RPA1 contains three other OB folds: DBD-A, DBD-B, and RPA1N. The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in DNA binding and trimerization. It contains two structural insertions not found to date in other OB-folds: a zinc ribbon and a three-helix bundle. RPA1 DBD-C also contains a Cys4-type zinc-binding motif, which plays a role in the ssDNA binding function of this domain. It appears that zinc itself may not be required for ssDNA binding. Pssm-ID: 239922 [Multi-domain] Cd Length: 166 Bit Score: 99.69 E-value: 1.73e-25
|
|||||||
RPA1_DBD_A_like | cd04480 | RPA1_DBD_A_like: A subgroup of uncharacterized plant OB folds with similarity to the second OB ... |
23-80 | 3.03e-13 | |||
RPA1_DBD_A_like: A subgroup of uncharacterized plant OB folds with similarity to the second OB fold, the ssDNA-binding domain (DBD)-A, of human RPA1 (also called RPA70). RPA1 is the large 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). In addition to DBD-A, RPA1 contains three other OB folds: DBD-B, DBD-C, and RPA1N. The major DNA binding activity of RPA is associated with DBD-A and DBD-B of RPA1. RPA1 DBD-C is involved in trimerization. The ssDNA-binding mechanism is believed to be multistep and to involve conformational change. Pssm-ID: 239926 [Multi-domain] Cd Length: 86 Bit Score: 64.20 E-value: 3.03e-13
|
|||||||
DUF223 | pfam02721 | Domain of unknown function DUF223; |
39-78 | 1.09e-03 | |||
Domain of unknown function DUF223; Pssm-ID: 145722 Cd Length: 95 Bit Score: 37.66 E-value: 1.09e-03
|
|||||||
Name | Accession | Description | Interval | E-value | |||
RPA1_DBD_C | cd04476 | RPA1_DBD_C: A subfamily of OB folds corresponding to the C-terminal OB fold, the ssDNA-binding ... |
110-252 | 1.73e-25 | |||
RPA1_DBD_C: A subfamily of OB folds corresponding to the C-terminal OB fold, the ssDNA-binding domain (DBD)-C, of human RPA1 (also called RPA70). RPA1 is the large 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). In addition to DBD-C, RPA1 contains three other OB folds: DBD-A, DBD-B, and RPA1N. The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in DNA binding and trimerization. It contains two structural insertions not found to date in other OB-folds: a zinc ribbon and a three-helix bundle. RPA1 DBD-C also contains a Cys4-type zinc-binding motif, which plays a role in the ssDNA binding function of this domain. It appears that zinc itself may not be required for ssDNA binding. Pssm-ID: 239922 [Multi-domain] Cd Length: 166 Bit Score: 99.69 E-value: 1.73e-25
|
|||||||
RPA1_DBD_A_like | cd04480 | RPA1_DBD_A_like: A subgroup of uncharacterized plant OB folds with similarity to the second OB ... |
23-80 | 3.03e-13 | |||
RPA1_DBD_A_like: A subgroup of uncharacterized plant OB folds with similarity to the second OB fold, the ssDNA-binding domain (DBD)-A, of human RPA1 (also called RPA70). RPA1 is the large 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). In addition to DBD-A, RPA1 contains three other OB folds: DBD-B, DBD-C, and RPA1N. The major DNA binding activity of RPA is associated with DBD-A and DBD-B of RPA1. RPA1 DBD-C is involved in trimerization. The ssDNA-binding mechanism is believed to be multistep and to involve conformational change. Pssm-ID: 239926 [Multi-domain] Cd Length: 86 Bit Score: 64.20 E-value: 3.03e-13
|
|||||||
DUF223 | pfam02721 | Domain of unknown function DUF223; |
39-78 | 1.09e-03 | |||
Domain of unknown function DUF223; Pssm-ID: 145722 Cd Length: 95 Bit Score: 37.66 E-value: 1.09e-03
|
|||||||
Blast search parameters | ||||
|