replication protein A 70 kDa DNA-binding subunit B-like [Prunus dulcis]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
RPA_2b-aaRSs_OBF_like super family | cl09930 | Replication protein A, class 2b aminoacyl-tRNA synthetases, and related proteins with ... |
138-247 | 1.53e-14 | ||||
Replication protein A, class 2b aminoacyl-tRNA synthetases, and related proteins with oligonucleotide/oligosaccharide (OB) fold.; This superfamily includes two oligonucleotide/oligosaccharide binding fold (OBF) domain families. One of these contains the OBF domains of the large (RPA1, 70kDa), middle (RPA2, RPA4, 32kDa) and small (RPA3, 14 kDa) subunits of human heterotrimeric Replication protein A (RPA), and similar domains. RPA is a nuclear single-strand (ss) DNA-binding protein involved in most aspects of DNA metabolism. This family includes the four OBF domains of RPA1 [DNA-binding domain (DBD)-A, DBD-B, DBD-C, and RPA1N], the OBF domain of RPA2 (RPA2 DBD-D), RPA3, and the OBF domain of RPA4. The major DNA binding activity of human RPA and Saccharomyces cerevisiae RPA appears to be associated with DBD-A and -B, of RPA1. RPA1 DBD-C shows only weak ssDNA-binding activity and is involved in trimerization. The other OBF domain family in this superfamily is the N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids to their cognate tRNAs during protein biosynthesis. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases. The actual alignment was detected with superfamily member cd04476: Pssm-ID: 471953 [Multi-domain] Cd Length: 166 Bit Score: 70.80 E-value: 1.53e-14
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rpa1 super family | cl36710 | replication factor-a protein 1 (rpa1); All proteins in this family for which functions are ... |
23-219 | 1.11e-11 | ||||
replication factor-a protein 1 (rpa1); All proteins in this family for which functions are known are part of a multiprotein complex made up of homologs of RPA1, RPA2 and RPA3 that bind ssDNA and function in the recognition of DNA damage for nucleotide excision repairThis family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] The actual alignment was detected with superfamily member TIGR00617: Pssm-ID: 273177 [Multi-domain] Cd Length: 608 Bit Score: 65.91 E-value: 1.11e-11
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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 ... |
138-247 | 1.53e-14 | ||||
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: 70.80 E-value: 1.53e-14
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rpa1 | TIGR00617 | replication factor-a protein 1 (rpa1); All proteins in this family for which functions are ... |
23-219 | 1.11e-11 | ||||
replication factor-a protein 1 (rpa1); All proteins in this family for which functions are known are part of a multiprotein complex made up of homologs of RPA1, RPA2 and RPA3 that bind ssDNA and function in the recognition of DNA damage for nucleotide excision repairThis family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273177 [Multi-domain] Cd Length: 608 Bit Score: 65.91 E-value: 1.11e-11
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RPA1_DBD_B | cd04475 | RPA1_DBD_B: A subfamily of OB folds corresponding to the third OB fold, the ssDNA-binding ... |
23-81 | 5.39e-10 | ||||
RPA1_DBD_B: A subfamily of OB folds corresponding to the third OB fold, the ssDNA-binding domain (DBD)-B, 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-B, RPA1 contains three other OB folds: DBD-A, DBD-C, and RPA1N. The major DNA binding activity of human RPA (hRPA) and Saccharomyces cerevisiae RPA (ScRPA) is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. Although ScRPA and the hRPA have similar ssDNA-binding properties, they differ functionally. Antibodies to hRPA do not cross-react with ScRPA, and null mutations in the ScRPA subunits are not complemented by corresponding human genes. Also, ScRPA cannot support Simian virus 40 (SV40) DNA replication in vitro, whereas human RPA can. Pssm-ID: 239921 [Multi-domain] Cd Length: 101 Bit Score: 56.05 E-value: 5.39e-10
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REPA_OB_2 | pfam16900 | Replication protein A OB domain; Replication protein A contains two OB domains in it's DNA ... |
23-76 | 2.71e-06 | ||||
Replication protein A OB domain; Replication protein A contains two OB domains in it's DNA binding region. This is the second of the OB domains. Pssm-ID: 465304 [Multi-domain] Cd Length: 98 Bit Score: 45.49 E-value: 2.71e-06
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Rep_fac-A_C | pfam08646 | Replication factor-A C terminal domain; This domain is found at the C terminal of replication ... |
138-223 | 1.46e-03 | ||||
Replication factor-A C terminal domain; This domain is found at the C terminal of replication factor A. Replication factor A (RPA) binds single-stranded DNA and is involved in replication, repair, and recombination of DNA. Pssm-ID: 462546 [Multi-domain] Cd Length: 146 Bit Score: 38.74 E-value: 1.46e-03
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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 ... |
138-247 | 1.53e-14 | ||||
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: 70.80 E-value: 1.53e-14
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rpa1 | TIGR00617 | replication factor-a protein 1 (rpa1); All proteins in this family for which functions are ... |
23-219 | 1.11e-11 | ||||
replication factor-a protein 1 (rpa1); All proteins in this family for which functions are known are part of a multiprotein complex made up of homologs of RPA1, RPA2 and RPA3 that bind ssDNA and function in the recognition of DNA damage for nucleotide excision repairThis family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273177 [Multi-domain] Cd Length: 608 Bit Score: 65.91 E-value: 1.11e-11
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RPA1_DBD_B | cd04475 | RPA1_DBD_B: A subfamily of OB folds corresponding to the third OB fold, the ssDNA-binding ... |
23-81 | 5.39e-10 | ||||
RPA1_DBD_B: A subfamily of OB folds corresponding to the third OB fold, the ssDNA-binding domain (DBD)-B, 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-B, RPA1 contains three other OB folds: DBD-A, DBD-C, and RPA1N. The major DNA binding activity of human RPA (hRPA) and Saccharomyces cerevisiae RPA (ScRPA) is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. Although ScRPA and the hRPA have similar ssDNA-binding properties, they differ functionally. Antibodies to hRPA do not cross-react with ScRPA, and null mutations in the ScRPA subunits are not complemented by corresponding human genes. Also, ScRPA cannot support Simian virus 40 (SV40) DNA replication in vitro, whereas human RPA can. Pssm-ID: 239921 [Multi-domain] Cd Length: 101 Bit Score: 56.05 E-value: 5.39e-10
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RPA1_DBD_B_like | cd04481 | RPA1_DBD_B_like: A subgroup of uncharacterized, plant OB folds with similarity to the third OB ... |
15-89 | 6.69e-07 | ||||
RPA1_DBD_B_like: A subgroup of uncharacterized, plant OB folds with similarity to the third OB fold, the ssDNA-binding domain (DBD)-B, 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-B, RPA1 contains three other OB folds: DBD-A, DBD-C, and RPA1N. The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B. RPA1 DBD-C is involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. Pssm-ID: 239927 [Multi-domain] Cd Length: 106 Bit Score: 47.27 E-value: 6.69e-07
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REPA_OB_2 | pfam16900 | Replication protein A OB domain; Replication protein A contains two OB domains in it's DNA ... |
23-76 | 2.71e-06 | ||||
Replication protein A OB domain; Replication protein A contains two OB domains in it's DNA binding region. This is the second of the OB domains. Pssm-ID: 465304 [Multi-domain] Cd Length: 98 Bit Score: 45.49 E-value: 2.71e-06
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Rep_fac-A_C | pfam08646 | Replication factor-A C terminal domain; This domain is found at the C terminal of replication ... |
138-223 | 1.46e-03 | ||||
Replication factor-A C terminal domain; This domain is found at the C terminal of replication factor A. Replication factor A (RPA) binds single-stranded DNA and is involved in replication, repair, and recombination of DNA. Pssm-ID: 462546 [Multi-domain] Cd Length: 146 Bit Score: 38.74 E-value: 1.46e-03
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Blast search parameters | ||||
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