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Conserved domains on  [gi|1242862519|ref|NP_001342344|]
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telomere-associated protein RIF1 isoform b [Mus musculus]

Protein Classification

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rif1_N pfam12231
Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is ...
 29-361 2.34e-94

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: 310.72  E-value: 2.34e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519   29 AYLTLTSRMTGEEGKEVIAEIEKNLSRLYTVLKAHISSQNSE-------LSSAALQALGFCLYNPRITSGLSEAN-IQEL 100
Cdd:pfam12231    1 AYMMLSRALKAYDNLPDRDALQDKMSLLCQFIQRDISSANSEtgpldssLVIQALKLLGTFLWNPAIASTLSDDFgVFII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  101 LLTLNGII-KSSDKNVCTRALWVISKQTFPAELV-SKMVSSIIDSLEVILSkgEIHSAVVDFEALNVIIRLIEQAPVQMG 178
Cdd:pfam12231   81 DHSIRSLEdPSTPKDIATHLLWVLSQQNFPPKIMtSDRVGRLLTALHNIEE--RVKGKSIIMERLNIYRRLLEQAPQLMA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  179 EESVRWAKLVIPLVVHSAQKVHLRgATALEMGMPLLLQKQQEIALITEHLMTTKL----------ISELQKLFKNK-NET 247
Cdd:pfam12231  159 AHADLWLPDLFTGMLSSVKDIRER-AISLGLEAALALGPEKEVSRAVLELLDRELedgktyieyyIERLQKMLKDKdNAV 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  248 YVLKLWPLFVKLLGKTLHR--SGSFINSLLQLEELGFRSGTPMIKKIAFIAWKSLIdnFALNPDILCSAKRLKLLMQPL- 324
Cdd:pfam12231  238 HVPQIWSVVILLLRKKRHSleSWEHFNEWLKLIQKCFNSSDPLTKIEANIAWNRLI--YALNPDESTSPKRLKLLCQPLl 315

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1242862519  325 ---------SSIHVRTETLALTKLEVWWYLLMRLGP--QLPANFEQVC 361
Cdd:pfam12231  316 sqlerkksdKSAPVLREAVLSSYCNLLYYAFRPGASheQLDLYWDEVV 363
Rif1_CTD_C-II_like cd14267
Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and ...
 2260-2307 8.86e-13

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: 64.54  E-value: 8.86e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1242862519 2260 NMWARGLGQLIRAKNIKTIGDLSTLTASEIKTLPIrspKVFNVKKALR 2307
Cdd:cd14267      1 PFWSRGLRQLVRALNIKTIGDLAQLSPEEKYNLPI---KLLTFMMALR 45
 
Name Accession Description Interval E-value
Rif1_N pfam12231
Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is ...
 29-361 2.34e-94

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: 310.72  E-value: 2.34e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519   29 AYLTLTSRMTGEEGKEVIAEIEKNLSRLYTVLKAHISSQNSE-------LSSAALQALGFCLYNPRITSGLSEAN-IQEL 100
Cdd:pfam12231    1 AYMMLSRALKAYDNLPDRDALQDKMSLLCQFIQRDISSANSEtgpldssLVIQALKLLGTFLWNPAIASTLSDDFgVFII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  101 LLTLNGII-KSSDKNVCTRALWVISKQTFPAELV-SKMVSSIIDSLEVILSkgEIHSAVVDFEALNVIIRLIEQAPVQMG 178
Cdd:pfam12231   81 DHSIRSLEdPSTPKDIATHLLWVLSQQNFPPKIMtSDRVGRLLTALHNIEE--RVKGKSIIMERLNIYRRLLEQAPQLMA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  179 EESVRWAKLVIPLVVHSAQKVHLRgATALEMGMPLLLQKQQEIALITEHLMTTKL----------ISELQKLFKNK-NET 247
Cdd:pfam12231  159 AHADLWLPDLFTGMLSSVKDIRER-AISLGLEAALALGPEKEVSRAVLELLDRELedgktyieyyIERLQKMLKDKdNAV 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  248 YVLKLWPLFVKLLGKTLHR--SGSFINSLLQLEELGFRSGTPMIKKIAFIAWKSLIdnFALNPDILCSAKRLKLLMQPL- 324
Cdd:pfam12231  238 HVPQIWSVVILLLRKKRHSleSWEHFNEWLKLIQKCFNSSDPLTKIEANIAWNRLI--YALNPDESTSPKRLKLLCQPLl 315

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1242862519  325 ---------SSIHVRTETLALTKLEVWWYLLMRLGP--QLPANFEQVC 361
Cdd:pfam12231  316 sqlerkksdKSAPVLREAVLSSYCNLLYYAFRPGASheQLDLYWDEVV 363
Rif1_CTD_C-II_like cd14267
Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and ...
 2260-2307 8.86e-13

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: 64.54  E-value: 8.86e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1242862519 2260 NMWARGLGQLIRAKNIKTIGDLSTLTASEIKTLPIrspKVFNVKKALR 2307
Cdd:cd14267      1 PFWSRGLRQLVRALNIKTIGDLAQLSPEEKYNLPI---KLLTFMMALR 45
 
Name Accession Description Interval E-value
Rif1_N pfam12231
Rap1-interacting factor 1 N terminal; This domain family is found in eukaryotes, and is ...
 29-361 2.34e-94

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: 310.72  E-value: 2.34e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519   29 AYLTLTSRMTGEEGKEVIAEIEKNLSRLYTVLKAHISSQNSE-------LSSAALQALGFCLYNPRITSGLSEAN-IQEL 100
Cdd:pfam12231    1 AYMMLSRALKAYDNLPDRDALQDKMSLLCQFIQRDISSANSEtgpldssLVIQALKLLGTFLWNPAIASTLSDDFgVFII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  101 LLTLNGII-KSSDKNVCTRALWVISKQTFPAELV-SKMVSSIIDSLEVILSkgEIHSAVVDFEALNVIIRLIEQAPVQMG 178
Cdd:pfam12231   81 DHSIRSLEdPSTPKDIATHLLWVLSQQNFPPKIMtSDRVGRLLTALHNIEE--RVKGKSIIMERLNIYRRLLEQAPQLMA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  179 EESVRWAKLVIPLVVHSAQKVHLRgATALEMGMPLLLQKQQEIALITEHLMTTKL----------ISELQKLFKNK-NET 247
Cdd:pfam12231  159 AHADLWLPDLFTGMLSSVKDIRER-AISLGLEAALALGPEKEVSRAVLELLDRELedgktyieyyIERLQKMLKDKdNAV 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862519  248 YVLKLWPLFVKLLGKTLHR--SGSFINSLLQLEELGFRSGTPMIKKIAFIAWKSLIdnFALNPDILCSAKRLKLLMQPL- 324
Cdd:pfam12231  238 HVPQIWSVVILLLRKKRHSleSWEHFNEWLKLIQKCFNSSDPLTKIEANIAWNRLI--YALNPDESTSPKRLKLLCQPLl 315

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1242862519  325 ---------SSIHVRTETLALTKLEVWWYLLMRLGP--QLPANFEQVC 361
Cdd:pfam12231  316 sqlerkksdKSAPVLREAVLSSYCNLLYYAFRPGASheQLDLYWDEVV 363
Rif1_CTD_C-II_like cd14267
Saccharomyces cerevisiae Rap1-interacting factor 1 CTD domain, metazoan Rif1 C-II domains and ...
 2260-2307 8.86e-13

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: 64.54  E-value: 8.86e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1242862519 2260 NMWARGLGQLIRAKNIKTIGDLSTLTASEIKTLPIrspKVFNVKKALR 2307
Cdd:cd14267      1 PFWSRGLRQLVRALNIKTIGDLAQLSPEEKYNLPI---KLLTFMMALR 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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