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telomere-associated protein RIF1 isoform X5 [Homo sapiens]
Rif1_N and Rif1_CTD_C-II_like domain-containing protein( domain architecture ID 13779819)
Rif1_N and Rif1_CTD_C-II_like domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||||
Rif1_N | pfam12231 | Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is ... |
1-325 | 6.03e-89 | ||||||
Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is typically between 135 and 146 amino acids in length. Rif1 is a protein which interacts with Rap1 to regulate telomere length. Interaction with telomeres limits their length. The N terminal region contains many HEAT- and ARMADILLO- type repeats. These are helical folds which form extended curved proteins or RNA interface surfaces. : Pssm-ID: 463499 Cd Length: 363 Bit Score: 294.93 E-value: 6.03e-89
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Rif1_CTD_C-II_like | cd14267 | Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and ... |
2276-2323 | 1.50e-12 | ||||||
Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and related domains; This model includes Saccharomyces cerevisiae Rif1_CTD (carboxy-terminal domain) and metazoan Rif1 C-II (C-terminal subdomain II). Rif1 was originally identified in S. cerevisiae where it negatively regulates telomere length homeostasis via interaction with the C-terminal domain of Rap1. A protective capping structure (telosome) comprised of Rap1, Rif1, and Rif2, inhibits telomerase, counteracts SIR-mediated transcriptional silencing, and prevents inadvertent recognition of telomeres as DNA double-strand breaks (DSBs). S. cerevisiae Rif1 has two Rap1 binding sites: the Rap1-binding module (RBM), and the CTD domain. The latter, represented here, has a lower Rap1 affinity, and provides trans binding through tetramerization. In mammals, Rif1 has been implicated in various cellular processes including pluripotency of stem cells, breast cancer development, and DSB repair pathway choice. A mutual antagonism between the nonhomologous end joining factors (53BP1-RIF1) and the homologous recombination factors (BRCA1 -CtIP) ensures correct repair pathway choice. : Pssm-ID: 341312 Cd Length: 46 Bit Score: 63.77 E-value: 1.50e-12
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Name | Accession | Description | Interval | E-value | ||||||
Rif1_N | pfam12231 | Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is ... |
1-325 | 6.03e-89 | ||||||
Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is typically between 135 and 146 amino acids in length. Rif1 is a protein which interacts with Rap1 to regulate telomere length. Interaction with telomeres limits their length. The N terminal region contains many HEAT- and ARMADILLO- type repeats. These are helical folds which form extended curved proteins or RNA interface surfaces. Pssm-ID: 463499 Cd Length: 363 Bit Score: 294.93 E-value: 6.03e-89
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Rif1_CTD_C-II_like | cd14267 | Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and ... |
2276-2323 | 1.50e-12 | ||||||
Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and related domains; This model includes Saccharomyces cerevisiae Rif1_CTD (carboxy-terminal domain) and metazoan Rif1 C-II (C-terminal subdomain II). Rif1 was originally identified in S. cerevisiae where it negatively regulates telomere length homeostasis via interaction with the C-terminal domain of Rap1. A protective capping structure (telosome) comprised of Rap1, Rif1, and Rif2, inhibits telomerase, counteracts SIR-mediated transcriptional silencing, and prevents inadvertent recognition of telomeres as DNA double-strand breaks (DSBs). S. cerevisiae Rif1 has two Rap1 binding sites: the Rap1-binding module (RBM), and the CTD domain. The latter, represented here, has a lower Rap1 affinity, and provides trans binding through tetramerization. In mammals, Rif1 has been implicated in various cellular processes including pluripotency of stem cells, breast cancer development, and DSB repair pathway choice. A mutual antagonism between the nonhomologous end joining factors (53BP1-RIF1) and the homologous recombination factors (BRCA1 -CtIP) ensures correct repair pathway choice. Pssm-ID: 341312 Cd Length: 46 Bit Score: 63.77 E-value: 1.50e-12
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Name | Accession | Description | Interval | E-value | ||||||
Rif1_N | pfam12231 | Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is ... |
1-325 | 6.03e-89 | ||||||
Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is typically between 135 and 146 amino acids in length. Rif1 is a protein which interacts with Rap1 to regulate telomere length. Interaction with telomeres limits their length. The N terminal region contains many HEAT- and ARMADILLO- type repeats. These are helical folds which form extended curved proteins or RNA interface surfaces. Pssm-ID: 463499 Cd Length: 363 Bit Score: 294.93 E-value: 6.03e-89
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Rif1_CTD_C-II_like | cd14267 | Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and ... |
2276-2323 | 1.50e-12 | ||||||
Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and related domains; This model includes Saccharomyces cerevisiae Rif1_CTD (carboxy-terminal domain) and metazoan Rif1 C-II (C-terminal subdomain II). Rif1 was originally identified in S. cerevisiae where it negatively regulates telomere length homeostasis via interaction with the C-terminal domain of Rap1. A protective capping structure (telosome) comprised of Rap1, Rif1, and Rif2, inhibits telomerase, counteracts SIR-mediated transcriptional silencing, and prevents inadvertent recognition of telomeres as DNA double-strand breaks (DSBs). S. cerevisiae Rif1 has two Rap1 binding sites: the Rap1-binding module (RBM), and the CTD domain. The latter, represented here, has a lower Rap1 affinity, and provides trans binding through tetramerization. In mammals, Rif1 has been implicated in various cellular processes including pluripotency of stem cells, breast cancer development, and DSB repair pathway choice. A mutual antagonism between the nonhomologous end joining factors (53BP1-RIF1) and the homologous recombination factors (BRCA1 -CtIP) ensures correct repair pathway choice. Pssm-ID: 341312 Cd Length: 46 Bit Score: 63.77 E-value: 1.50e-12
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Blast search parameters | ||||
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